A common pentapeptide conformation occurs in viral acid proteases and other proteins
We found a pentapeptide conformation, termed a type I twist, which has a strikingly high propensity (56%) for aspartic acid in the first position. Type I twists include the active site loops from cellular and viral aspartic proteases, with the catalytic Asp in the first position. Fifteen other type...
Gespeichert in:
| Veröffentlicht in: | Journal of molecular biology 1990-11, Vol.216 (2), p.201-206 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 206 |
|---|---|
| container_issue | 2 |
| container_start_page | 201 |
| container_title | Journal of molecular biology |
| container_volume | 216 |
| creator | Karpen, Mary E. Neet, Kenneth E. de Haseth, Pieter L. |
| description | We found a pentapeptide conformation, termed a type I twist, which has a strikingly high propensity (56%) for aspartic acid in the first position. Type I twists include the active site loops from cellular and viral aspartic proteases, with the catalytic Asp in the first position. Fifteen other type I twists, from non-homologous proteins, were found among high-resolution structures in the Protein Data Bank using a comparison method based on main-chain torsion angles. We propose that the Asp affects electrostatic interactions and thus plays a major structural role in the formation of this recurring motif, in addition to its catalytic role in the aspartic proteases. |
| doi_str_mv | 10.1016/S0022-2836(05)80307-9 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80160899</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0022283605803079</els_id><sourcerecordid>15818891</sourcerecordid><originalsourceid>FETCH-LOGICAL-c421t-ec16dc7c5139c20fce3babe37c4eddb716345a7613fa9f6d757e97510af45fff3</originalsourceid><addsrcrecordid>eNqFkE1rFTEUhoMo9fbjJxRmo9TFaD4mmWQlpdQqFFxY1yH35AQjM8mYzC34783tvdRlV4HzPjnv4SHkktGPjDL16QelnPdcC3VF5QdNBR1784psGNWm10ro12TzjLwlp7X-ppRKMegTcsK5HAwzG_Jw3UGe55y6BdPqFlzW6LHNUshldmtsSQbYldrF1D3G4qbOQfTdUvKKrmLtXPJdXn9hOcxiqufkTXBTxYvje0Z-frl9uPna33-_-3Zzfd_DwNnaIzDlYQTJhAFOA6DYui2KEQb0fjsyJQbpRsVEcCYoP8oRzSgZdWGQIQRxRt4f9rbiPzusq51jBZwmlzDvqtXNU7NhXgSZ1ExrwxooDyCUXGvBYJcSZ1f-WkbtXrt90m73Ti2V9km73RdcHgt22xn986-j55a_O-augptCcQli_b_cDEpxPjTu84HDpu0xYrEVIiZAHwvCan2OL1zyDxcjn_s</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>15818891</pqid></control><display><type>article</type><title>A common pentapeptide conformation occurs in viral acid proteases and other proteins</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Karpen, Mary E. ; Neet, Kenneth E. ; de Haseth, Pieter L.</creator><creatorcontrib>Karpen, Mary E. ; Neet, Kenneth E. ; de Haseth, Pieter L.</creatorcontrib><description>We found a pentapeptide conformation, termed a type I twist, which has a strikingly high propensity (56%) for aspartic acid in the first position. Type I twists include the active site loops from cellular and viral aspartic proteases, with the catalytic Asp in the first position. Fifteen other type I twists, from non-homologous proteins, were found among high-resolution structures in the Protein Data Bank using a comparison method based on main-chain torsion angles. We propose that the Asp affects electrostatic interactions and thus plays a major structural role in the formation of this recurring motif, in addition to its catalytic role in the aspartic proteases.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/S0022-2836(05)80307-9</identifier><identifier>PMID: 2254919</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier Ltd</publisher><subject>Amino Acid Sequence ; aspartic proteinase ; Biological and medical sciences ; Databases, Factual ; Endopeptidases - genetics ; Fundamental and applied biological sciences. Psychology ; Microbiology ; Models, Molecular ; Molecular Sequence Data ; Morphology, structure, chemical composition, physicochemical properties ; Protein Conformation ; Sequence Homology, Nucleic Acid ; Viral Proteins - genetics ; Virology ; viruses ; Viruses - enzymology ; Viruses - genetics</subject><ispartof>Journal of molecular biology, 1990-11, Vol.216 (2), p.201-206</ispartof><rights>1990 Academic Press Limited</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c421t-ec16dc7c5139c20fce3babe37c4eddb716345a7613fa9f6d757e97510af45fff3</citedby><cites>FETCH-LOGICAL-c421t-ec16dc7c5139c20fce3babe37c4eddb716345a7613fa9f6d757e97510af45fff3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022283605803079$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19466224$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2254919$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Karpen, Mary E.</creatorcontrib><creatorcontrib>Neet, Kenneth E.</creatorcontrib><creatorcontrib>de Haseth, Pieter L.</creatorcontrib><title>A common pentapeptide conformation occurs in viral acid proteases and other proteins</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>We found a pentapeptide conformation, termed a type I twist, which has a strikingly high propensity (56%) for aspartic acid in the first position. Type I twists include the active site loops from cellular and viral aspartic proteases, with the catalytic Asp in the first position. Fifteen other type I twists, from non-homologous proteins, were found among high-resolution structures in the Protein Data Bank using a comparison method based on main-chain torsion angles. We propose that the Asp affects electrostatic interactions and thus plays a major structural role in the formation of this recurring motif, in addition to its catalytic role in the aspartic proteases.</description><subject>Amino Acid Sequence</subject><subject>aspartic proteinase</subject><subject>Biological and medical sciences</subject><subject>Databases, Factual</subject><subject>Endopeptidases - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Microbiology</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Protein Conformation</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Viral Proteins - genetics</subject><subject>Virology</subject><subject>viruses</subject><subject>Viruses - enzymology</subject><subject>Viruses - genetics</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rFTEUhoMo9fbjJxRmo9TFaD4mmWQlpdQqFFxY1yH35AQjM8mYzC34783tvdRlV4HzPjnv4SHkktGPjDL16QelnPdcC3VF5QdNBR1784psGNWm10ro12TzjLwlp7X-ppRKMegTcsK5HAwzG_Jw3UGe55y6BdPqFlzW6LHNUshldmtsSQbYldrF1D3G4qbOQfTdUvKKrmLtXPJdXn9hOcxiqufkTXBTxYvje0Z-frl9uPna33-_-3Zzfd_DwNnaIzDlYQTJhAFOA6DYui2KEQb0fjsyJQbpRsVEcCYoP8oRzSgZdWGQIQRxRt4f9rbiPzusq51jBZwmlzDvqtXNU7NhXgSZ1ExrwxooDyCUXGvBYJcSZ1f-WkbtXrt90m73Ti2V9km73RdcHgt22xn986-j55a_O-augptCcQli_b_cDEpxPjTu84HDpu0xYrEVIiZAHwvCan2OL1zyDxcjn_s</recordid><startdate>19901120</startdate><enddate>19901120</enddate><creator>Karpen, Mary E.</creator><creator>Neet, Kenneth E.</creator><creator>de Haseth, Pieter L.</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>IQODW</scope><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>7QL</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19901120</creationdate><title>A common pentapeptide conformation occurs in viral acid proteases and other proteins</title><author>Karpen, Mary E. ; Neet, Kenneth E. ; de Haseth, Pieter L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c421t-ec16dc7c5139c20fce3babe37c4eddb716345a7613fa9f6d757e97510af45fff3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>aspartic proteinase</topic><topic>Biological and medical sciences</topic><topic>Databases, Factual</topic><topic>Endopeptidases - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Protein Conformation</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Viral Proteins - genetics</topic><topic>Virology</topic><topic>viruses</topic><topic>Viruses - enzymology</topic><topic>Viruses - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Karpen, Mary E.</creatorcontrib><creatorcontrib>Neet, Kenneth E.</creatorcontrib><creatorcontrib>de Haseth, Pieter L.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Karpen, Mary E.</au><au>Neet, Kenneth E.</au><au>de Haseth, Pieter L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A common pentapeptide conformation occurs in viral acid proteases and other proteins</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1990-11-20</date><risdate>1990</risdate><volume>216</volume><issue>2</issue><spage>201</spage><epage>206</epage><pages>201-206</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>We found a pentapeptide conformation, termed a type I twist, which has a strikingly high propensity (56%) for aspartic acid in the first position. Type I twists include the active site loops from cellular and viral aspartic proteases, with the catalytic Asp in the first position. Fifteen other type I twists, from non-homologous proteins, were found among high-resolution structures in the Protein Data Bank using a comparison method based on main-chain torsion angles. We propose that the Asp affects electrostatic interactions and thus plays a major structural role in the formation of this recurring motif, in addition to its catalytic role in the aspartic proteases.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>2254919</pmid><doi>10.1016/S0022-2836(05)80307-9</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1990-11, Vol.216 (2), p.201-206 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80160899 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Amino Acid Sequence aspartic proteinase Biological and medical sciences Databases, Factual Endopeptidases - genetics Fundamental and applied biological sciences. Psychology Microbiology Models, Molecular Molecular Sequence Data Morphology, structure, chemical composition, physicochemical properties Protein Conformation Sequence Homology, Nucleic Acid Viral Proteins - genetics Virology viruses Viruses - enzymology Viruses - genetics |
| title | A common pentapeptide conformation occurs in viral acid proteases and other proteins |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T07%3A24%3A49IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20common%20pentapeptide%20conformation%20occurs%20in%20viral%20acid%20proteases%20and%20other%20proteins&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=Karpen,%20Mary%20E.&rft.date=1990-11-20&rft.volume=216&rft.issue=2&rft.spage=201&rft.epage=206&rft.pages=201-206&rft.issn=0022-2836&rft.eissn=1089-8638&rft.coden=JMOBAK&rft_id=info:doi/10.1016/S0022-2836(05)80307-9&rft_dat=%3Cproquest_cross%3E15818891%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=15818891&rft_id=info:pmid/2254919&rft_els_id=S0022283605803079&rfr_iscdi=true |