Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein
Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule consists of two CUB domains followed by a C-terminal NTR...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2003-02, Vol.278 (9), p.7199-7205 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 7205 |
|---|---|
| container_issue | 9 |
| container_start_page | 7199 |
| container_title | The Journal of biological chemistry |
| container_volume | 278 |
| creator | Bernocco, Simonetta Steiglitz, Barry M Svergun, Dmitri I Petoukhov, Maxim V Ruggiero, Florence Ricard-Blum, Sylvie Ebel, Christine Geourjon, Christophe Deleage, Gilbert Font, Bernard Eichenberger, Denise Greenspan, Daniel S Hulmes, David J S |
| description | Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid
metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule
consists of two CUB domains followed by a C-terminal NTR (netrin-like) domain. In order to obtain structural insights into
the function of PCPE, the recombinant protein was characterized by a range of biophysical techniques, including analytical
ultracentrifugation, transmission electron microscopy, and small angle x-ray scattering. All three approaches showed PCPE
to be a rod-like molecule, with a length of â¼150 Ã
. Homology modeling of both CUB domains and the NTR domain was consistent
with the low-resolution structure of PCPE deduced from the small angle x-ray scattering data. Comparison with the low-resolution
structure of the procollagen C-terminal region supports a recently proposed model (Ricard-Blum, S., Bernocco, S., Font, B.,
Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. (2002) J. Biol. Chem. 277, 33864â33869) for the mechanism of action of PCPE. |
| doi_str_mv | 10.1074/jbc.M210857200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_00313745v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73037110</sourcerecordid><originalsourceid>FETCH-LOGICAL-c392t-5bd4258982217c80062af11bbdddeab4a702bea8032dabe2a3bf302e2c3f40403</originalsourceid><addsrcrecordid>eNpFkU1v1DAQhi0EotvClSOyOCBxyDK2kyY5VsvSIm0F4kPiZtnOZOMqsYvtsGp_PV5lRecyH3rm1YxeQt4wWDOoy4932qxvOYOmqjnAM7LKpShExX4_JysAzoqWV80ZOY_xDnKULXtJzhgvm0smmhV53PkD_Y7Rj3Oy3tEfKcwmzQHpJ0wYJuvUMh_8IdJvwRs_jmqPjm6K3CXMQES6dYNyBgNNnmqkytHt6N1eJezo7Twm2_lJWUevxwfj75e9V-RFr8aIr0_5gvz6vP25uSl2X6-_bK52hREtT0WluzK_0Dacs9o0AJdc9Yxp3XUdKl2qGrhG1YDgndLIldC9AI7ciL6EEsQF-bDoDmqU98FOKjxIr6y8udrJ4wxAMFGX1V-W2fcLm2_8M2NMcrLRYH7ZoZ-jrAWImrGj6HoBTfAxBuz_KzOQR2dkdkY-OZMX3p6UZz1h94SfrMjAu9OZdj8cbECprTcDTpLXjWxlzdpW_APqPpaG</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>73037110</pqid></control><display><type>article</type><title>Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein</title><source>MEDLINE</source><source>Alma/SFX Local Collection</source><source>EZB Electronic Journals Library</source><creator>Bernocco, Simonetta ; Steiglitz, Barry M ; Svergun, Dmitri I ; Petoukhov, Maxim V ; Ruggiero, Florence ; Ricard-Blum, Sylvie ; Ebel, Christine ; Geourjon, Christophe ; Deleage, Gilbert ; Font, Bernard ; Eichenberger, Denise ; Greenspan, Daniel S ; Hulmes, David J S</creator><creatorcontrib>Bernocco, Simonetta ; Steiglitz, Barry M ; Svergun, Dmitri I ; Petoukhov, Maxim V ; Ruggiero, Florence ; Ricard-Blum, Sylvie ; Ebel, Christine ; Geourjon, Christophe ; Deleage, Gilbert ; Font, Bernard ; Eichenberger, Denise ; Greenspan, Daniel S ; Hulmes, David J S</creatorcontrib><description>Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid
metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule
consists of two CUB domains followed by a C-terminal NTR (netrin-like) domain. In order to obtain structural insights into
the function of PCPE, the recombinant protein was characterized by a range of biophysical techniques, including analytical
ultracentrifugation, transmission electron microscopy, and small angle x-ray scattering. All three approaches showed PCPE
to be a rod-like molecule, with a length of â¼150 Ã
. Homology modeling of both CUB domains and the NTR domain was consistent
with the low-resolution structure of PCPE deduced from the small angle x-ray scattering data. Comparison with the low-resolution
structure of the procollagen C-terminal region supports a recently proposed model (Ricard-Blum, S., Bernocco, S., Font, B.,
Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. (2002) J. Biol. Chem. 277, 33864â33869) for the mechanism of action of PCPE.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M210857200</identifier><identifier>PMID: 12486138</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Biochemistry, Molecular Biology ; Cell Line ; Extracellular Matrix Proteins ; Glycoproteins ; Glycoproteins - chemistry ; Glycoproteins - ultrastructure ; Humans ; Life Sciences ; Mass Spectrometry ; Microscopy, Electron ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Recombinant Proteins ; Recombinant Proteins - metabolism ; Scattering, Radiation ; Sequence Homology, Amino Acid ; Ultracentrifugation ; X-Rays</subject><ispartof>The Journal of biological chemistry, 2003-02, Vol.278 (9), p.7199-7205</ispartof><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-5bd4258982217c80062af11bbdddeab4a702bea8032dabe2a3bf302e2c3f40403</citedby><cites>FETCH-LOGICAL-c392t-5bd4258982217c80062af11bbdddeab4a702bea8032dabe2a3bf302e2c3f40403</cites><orcidid>0000-0003-2915-5359 ; 0000-0002-6912-500X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12486138$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-00313745$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Bernocco, Simonetta</creatorcontrib><creatorcontrib>Steiglitz, Barry M</creatorcontrib><creatorcontrib>Svergun, Dmitri I</creatorcontrib><creatorcontrib>Petoukhov, Maxim V</creatorcontrib><creatorcontrib>Ruggiero, Florence</creatorcontrib><creatorcontrib>Ricard-Blum, Sylvie</creatorcontrib><creatorcontrib>Ebel, Christine</creatorcontrib><creatorcontrib>Geourjon, Christophe</creatorcontrib><creatorcontrib>Deleage, Gilbert</creatorcontrib><creatorcontrib>Font, Bernard</creatorcontrib><creatorcontrib>Eichenberger, Denise</creatorcontrib><creatorcontrib>Greenspan, Daniel S</creatorcontrib><creatorcontrib>Hulmes, David J S</creatorcontrib><title>Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid
metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule
consists of two CUB domains followed by a C-terminal NTR (netrin-like) domain. In order to obtain structural insights into
the function of PCPE, the recombinant protein was characterized by a range of biophysical techniques, including analytical
ultracentrifugation, transmission electron microscopy, and small angle x-ray scattering. All three approaches showed PCPE
to be a rod-like molecule, with a length of â¼150 Ã
. Homology modeling of both CUB domains and the NTR domain was consistent
with the low-resolution structure of PCPE deduced from the small angle x-ray scattering data. Comparison with the low-resolution
structure of the procollagen C-terminal region supports a recently proposed model (Ricard-Blum, S., Bernocco, S., Font, B.,
Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. (2002) J. Biol. Chem. 277, 33864â33869) for the mechanism of action of PCPE.</description><subject>Amino Acid Sequence</subject><subject>Biochemistry, Molecular Biology</subject><subject>Cell Line</subject><subject>Extracellular Matrix Proteins</subject><subject>Glycoproteins</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - ultrastructure</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Mass Spectrometry</subject><subject>Microscopy, Electron</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Proteins</subject><subject>Recombinant Proteins - metabolism</subject><subject>Scattering, Radiation</subject><subject>Sequence Homology, Amino Acid</subject><subject>Ultracentrifugation</subject><subject>X-Rays</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkU1v1DAQhi0EotvClSOyOCBxyDK2kyY5VsvSIm0F4kPiZtnOZOMqsYvtsGp_PV5lRecyH3rm1YxeQt4wWDOoy4932qxvOYOmqjnAM7LKpShExX4_JysAzoqWV80ZOY_xDnKULXtJzhgvm0smmhV53PkD_Y7Rj3Oy3tEfKcwmzQHpJ0wYJuvUMh_8IdJvwRs_jmqPjm6K3CXMQES6dYNyBgNNnmqkytHt6N1eJezo7Twm2_lJWUevxwfj75e9V-RFr8aIr0_5gvz6vP25uSl2X6-_bK52hREtT0WluzK_0Dacs9o0AJdc9Yxp3XUdKl2qGrhG1YDgndLIldC9AI7ciL6EEsQF-bDoDmqU98FOKjxIr6y8udrJ4wxAMFGX1V-W2fcLm2_8M2NMcrLRYH7ZoZ-jrAWImrGj6HoBTfAxBuz_KzOQR2dkdkY-OZMX3p6UZz1h94SfrMjAu9OZdj8cbECprTcDTpLXjWxlzdpW_APqPpaG</recordid><startdate>20030228</startdate><enddate>20030228</enddate><creator>Bernocco, Simonetta</creator><creator>Steiglitz, Barry M</creator><creator>Svergun, Dmitri I</creator><creator>Petoukhov, Maxim V</creator><creator>Ruggiero, Florence</creator><creator>Ricard-Blum, Sylvie</creator><creator>Ebel, Christine</creator><creator>Geourjon, Christophe</creator><creator>Deleage, Gilbert</creator><creator>Font, Bernard</creator><creator>Eichenberger, Denise</creator><creator>Greenspan, Daniel S</creator><creator>Hulmes, David J S</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-2915-5359</orcidid><orcidid>https://orcid.org/0000-0002-6912-500X</orcidid></search><sort><creationdate>20030228</creationdate><title>Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein</title><author>Bernocco, Simonetta ; Steiglitz, Barry M ; Svergun, Dmitri I ; Petoukhov, Maxim V ; Ruggiero, Florence ; Ricard-Blum, Sylvie ; Ebel, Christine ; Geourjon, Christophe ; Deleage, Gilbert ; Font, Bernard ; Eichenberger, Denise ; Greenspan, Daniel S ; Hulmes, David J S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-5bd4258982217c80062af11bbdddeab4a702bea8032dabe2a3bf302e2c3f40403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Biochemistry, Molecular Biology</topic><topic>Cell Line</topic><topic>Extracellular Matrix Proteins</topic><topic>Glycoproteins</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - ultrastructure</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Mass Spectrometry</topic><topic>Microscopy, Electron</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Conformation</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Proteins</topic><topic>Recombinant Proteins - metabolism</topic><topic>Scattering, Radiation</topic><topic>Sequence Homology, Amino Acid</topic><topic>Ultracentrifugation</topic><topic>X-Rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bernocco, Simonetta</creatorcontrib><creatorcontrib>Steiglitz, Barry M</creatorcontrib><creatorcontrib>Svergun, Dmitri I</creatorcontrib><creatorcontrib>Petoukhov, Maxim V</creatorcontrib><creatorcontrib>Ruggiero, Florence</creatorcontrib><creatorcontrib>Ricard-Blum, Sylvie</creatorcontrib><creatorcontrib>Ebel, Christine</creatorcontrib><creatorcontrib>Geourjon, Christophe</creatorcontrib><creatorcontrib>Deleage, Gilbert</creatorcontrib><creatorcontrib>Font, Bernard</creatorcontrib><creatorcontrib>Eichenberger, Denise</creatorcontrib><creatorcontrib>Greenspan, Daniel S</creatorcontrib><creatorcontrib>Hulmes, David J S</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bernocco, Simonetta</au><au>Steiglitz, Barry M</au><au>Svergun, Dmitri I</au><au>Petoukhov, Maxim V</au><au>Ruggiero, Florence</au><au>Ricard-Blum, Sylvie</au><au>Ebel, Christine</au><au>Geourjon, Christophe</au><au>Deleage, Gilbert</au><au>Font, Bernard</au><au>Eichenberger, Denise</au><au>Greenspan, Daniel S</au><au>Hulmes, David J S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2003-02-28</date><risdate>2003</risdate><volume>278</volume><issue>9</issue><spage>7199</spage><epage>7205</epage><pages>7199-7205</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Procollagen C-proteinase enhancer (PCPE) is an extracellular matrix glycoprotein that can stimulate the action of tolloid
metalloproteinases, such as bone morphogenetic protein-1, on a procollagen substrate, by up to 20-fold. The PCPE molecule
consists of two CUB domains followed by a C-terminal NTR (netrin-like) domain. In order to obtain structural insights into
the function of PCPE, the recombinant protein was characterized by a range of biophysical techniques, including analytical
ultracentrifugation, transmission electron microscopy, and small angle x-ray scattering. All three approaches showed PCPE
to be a rod-like molecule, with a length of â¼150 Ã
. Homology modeling of both CUB domains and the NTR domain was consistent
with the low-resolution structure of PCPE deduced from the small angle x-ray scattering data. Comparison with the low-resolution
structure of the procollagen C-terminal region supports a recently proposed model (Ricard-Blum, S., Bernocco, S., Font, B.,
Moali, C., Eichenberger, D., Farjanel, J., Burchardt, E. R., van der Rest, M., Kessler, E., and Hulmes, D. J. S. (2002) J. Biol. Chem. 277, 33864â33869) for the mechanism of action of PCPE.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>12486138</pmid><doi>10.1074/jbc.M210857200</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0003-2915-5359</orcidid><orcidid>https://orcid.org/0000-0002-6912-500X</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2003-02, Vol.278 (9), p.7199-7205 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_00313745v1 |
| source | MEDLINE; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Amino Acid Sequence Biochemistry, Molecular Biology Cell Line Extracellular Matrix Proteins Glycoproteins Glycoproteins - chemistry Glycoproteins - ultrastructure Humans Life Sciences Mass Spectrometry Microscopy, Electron Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Tertiary Recombinant Proteins Recombinant Proteins - metabolism Scattering, Radiation Sequence Homology, Amino Acid Ultracentrifugation X-Rays |
| title | Low Resolution Structure Determination Shows Procollagen C-Proteinase Enhancer to be an Elongated Multidomain Glycoprotein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T14%3A49%3A34IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Low%20Resolution%20Structure%20Determination%20Shows%20Procollagen%20C-Proteinase%20Enhancer%20to%20be%20an%20Elongated%20Multidomain%20Glycoprotein&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Bernocco,%20Simonetta&rft.date=2003-02-28&rft.volume=278&rft.issue=9&rft.spage=7199&rft.epage=7205&rft.pages=7199-7205&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M210857200&rft_dat=%3Cproquest_hal_p%3E73037110%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=73037110&rft_id=info:pmid/12486138&rfr_iscdi=true |