Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A
Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391–414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385–414, 380–414 and 374–414 of calcineurin A were used for this aim....
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2004-08, Vol.573 (1), p.121-126 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 126 |
|---|---|
| container_issue | 1 |
| container_start_page | 121 |
| container_title | FEBS letters |
| container_volume | 573 |
| creator | Noguchi, Masahiro Izumi, Yoshinobu Yoshino, Hidenori |
| description | Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391–414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385–414, 380–414 and 374–414 of calcineurin A were used for this aim. The X-ray data are consistent with the fact that calmodulin binds all three peptides with or without Ca
2+. Without Ca
2+, the whole peptide including acid residues interacts with dumbbell shaped calmodulin, while the acid region is extruded from globular shaped calmodulin with Ca
2+. Consequently, a conformation of sequence 374–414 in calcineurin might be changed by Ca
2+-signal via calmodulin, suggesting the consequence of this region with acid residues in the full activation mechanism of calcineurin by Ca
2+-bound calmodulin. |
| doi_str_mv | 10.1016/j.febslet.2004.07.079 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_66816512</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579304009536</els_id><sourcerecordid>19715975</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4576-547ebc963743692d841f19cf727f318f43963b924c9d6ff99a52538896839b4a3</originalsourceid><addsrcrecordid>eNqNkU1r3DAQhkVpaLZpf0KLT715I1nfvZQk5KMQyKHpWdjyyNViS6lkp-y_r9xdyDGFATHM874z6EXoE8Fbgok4320ddHmEedtgzLZYltJv0IYoSWvKhHqLNhgTVnOp6Sl6n_MOl14R_Q6dEk4bqZXYoOfHNg0wVwlsHIKffQxVt69sO06xX0YfvlbzL6hSHKGKrmqt7ws7rJiNYfbDEpdczfEf9aKqOx96H4aqj1PrwyotQ-sDLKm0Fx_QiWvHDB-P7xn6eXP9eHVX3z_cfr-6uK8t41LUnEnorBZUMip00ytGHNHWyUY6SpRjtMw63TCre-Gc1i1vOFVKC0V1x1p6hr4cfJ9S_L1Ans3ks4VxbAOUw40QighOmldBoiXhWvIC8gNoU8w5gTNPyU9t2huCzZqM2ZljMmZNxmBZShfd5-OCpZugf1EdoyjA3QH440fY_5-rubm-bH6sMa8pY4ax5nS1-nawgvK1zx6SydZDsND7kvNs-uhfufYv3Um3vw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19715975</pqid></control><display><type>article</type><title>Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Wiley Free Content</source><source>ScienceDirect Journals (5 years ago - present)</source><source>Wiley Online Library All Journals</source><source>Alma/SFX Local Collection</source><creator>Noguchi, Masahiro ; Izumi, Yoshinobu ; Yoshino, Hidenori</creator><creatorcontrib>Noguchi, Masahiro ; Izumi, Yoshinobu ; Yoshino, Hidenori</creatorcontrib><description>Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391–414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385–414, 380–414 and 374–414 of calcineurin A were used for this aim. The X-ray data are consistent with the fact that calmodulin binds all three peptides with or without Ca
2+. Without Ca
2+, the whole peptide including acid residues interacts with dumbbell shaped calmodulin, while the acid region is extruded from globular shaped calmodulin with Ca
2+. Consequently, a conformation of sequence 374–414 in calcineurin might be changed by Ca
2+-signal via calmodulin, suggesting the consequence of this region with acid residues in the full activation mechanism of calcineurin by Ca
2+-bound calmodulin.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2004.07.079</identifier><identifier>PMID: 15327986</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acids - chemistry ; Acids - metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Ca 2+-induced extrusion ; Ca2+-induced extrusion ; Calcineurin ; Calcineurin - chemistry ; Calcineurin - metabolism ; Calcium - metabolism ; Calcium - pharmacology ; Calmodulin ; Calmodulin - metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Rats ; Small-angle X-ray scattering ; Static Electricity ; Substrate Specificity ; X-Ray Diffraction</subject><ispartof>FEBS letters, 2004-08, Vol.573 (1), p.121-126</ispartof><rights>2004 Federation of European Biochemical Societies</rights><rights>FEBS Letters 573 (2004) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4576-547ebc963743692d841f19cf727f318f43963b924c9d6ff99a52538896839b4a3</citedby><cites>FETCH-LOGICAL-c4576-547ebc963743692d841f19cf727f318f43963b924c9d6ff99a52538896839b4a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2004.07.079$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2004.07.079$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1416,1432,3548,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15327986$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Noguchi, Masahiro</creatorcontrib><creatorcontrib>Izumi, Yoshinobu</creatorcontrib><creatorcontrib>Yoshino, Hidenori</creatorcontrib><title>Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391–414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385–414, 380–414 and 374–414 of calcineurin A were used for this aim. The X-ray data are consistent with the fact that calmodulin binds all three peptides with or without Ca
2+. Without Ca
2+, the whole peptide including acid residues interacts with dumbbell shaped calmodulin, while the acid region is extruded from globular shaped calmodulin with Ca
2+. Consequently, a conformation of sequence 374–414 in calcineurin might be changed by Ca
2+-signal via calmodulin, suggesting the consequence of this region with acid residues in the full activation mechanism of calcineurin by Ca
2+-bound calmodulin.</description><subject>Acids - chemistry</subject><subject>Acids - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Ca 2+-induced extrusion</subject><subject>Ca2+-induced extrusion</subject><subject>Calcineurin</subject><subject>Calcineurin - chemistry</subject><subject>Calcineurin - metabolism</subject><subject>Calcium - metabolism</subject><subject>Calcium - pharmacology</subject><subject>Calmodulin</subject><subject>Calmodulin - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Rats</subject><subject>Small-angle X-ray scattering</subject><subject>Static Electricity</subject><subject>Substrate Specificity</subject><subject>X-Ray Diffraction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1r3DAQhkVpaLZpf0KLT715I1nfvZQk5KMQyKHpWdjyyNViS6lkp-y_r9xdyDGFATHM874z6EXoE8Fbgok4320ddHmEedtgzLZYltJv0IYoSWvKhHqLNhgTVnOp6Sl6n_MOl14R_Q6dEk4bqZXYoOfHNg0wVwlsHIKffQxVt69sO06xX0YfvlbzL6hSHKGKrmqt7ws7rJiNYfbDEpdczfEf9aKqOx96H4aqj1PrwyotQ-sDLKm0Fx_QiWvHDB-P7xn6eXP9eHVX3z_cfr-6uK8t41LUnEnorBZUMip00ytGHNHWyUY6SpRjtMw63TCre-Gc1i1vOFVKC0V1x1p6hr4cfJ9S_L1Ans3ks4VxbAOUw40QighOmldBoiXhWvIC8gNoU8w5gTNPyU9t2huCzZqM2ZljMmZNxmBZShfd5-OCpZugf1EdoyjA3QH440fY_5-rubm-bH6sMa8pY4ax5nS1-nawgvK1zx6SydZDsND7kvNs-uhfufYv3Um3vw</recordid><startdate>20040827</startdate><enddate>20040827</enddate><creator>Noguchi, Masahiro</creator><creator>Izumi, Yoshinobu</creator><creator>Yoshino, Hidenori</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7QP</scope><scope>7X8</scope></search><sort><creationdate>20040827</creationdate><title>Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A</title><author>Noguchi, Masahiro ; Izumi, Yoshinobu ; Yoshino, Hidenori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4576-547ebc963743692d841f19cf727f318f43963b924c9d6ff99a52538896839b4a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acids - chemistry</topic><topic>Acids - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Ca 2+-induced extrusion</topic><topic>Ca2+-induced extrusion</topic><topic>Calcineurin</topic><topic>Calcineurin - chemistry</topic><topic>Calcineurin - metabolism</topic><topic>Calcium - metabolism</topic><topic>Calcium - pharmacology</topic><topic>Calmodulin</topic><topic>Calmodulin - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Rats</topic><topic>Small-angle X-ray scattering</topic><topic>Static Electricity</topic><topic>Substrate Specificity</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Noguchi, Masahiro</creatorcontrib><creatorcontrib>Izumi, Yoshinobu</creatorcontrib><creatorcontrib>Yoshino, Hidenori</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Noguchi, Masahiro</au><au>Izumi, Yoshinobu</au><au>Yoshino, Hidenori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-08-27</date><risdate>2004</risdate><volume>573</volume><issue>1</issue><spage>121</spage><epage>126</epage><pages>121-126</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Small-angle X-ray scattering was used to investigate the role of acid region contiguous to the calmodulin-binding domain (391–414) of calcineurin in the target recognition by calmodulin. Three synthetic peptides with the residues 385–414, 380–414 and 374–414 of calcineurin A were used for this aim. The X-ray data are consistent with the fact that calmodulin binds all three peptides with or without Ca
2+. Without Ca
2+, the whole peptide including acid residues interacts with dumbbell shaped calmodulin, while the acid region is extruded from globular shaped calmodulin with Ca
2+. Consequently, a conformation of sequence 374–414 in calcineurin might be changed by Ca
2+-signal via calmodulin, suggesting the consequence of this region with acid residues in the full activation mechanism of calcineurin by Ca
2+-bound calmodulin.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15327986</pmid><doi>10.1016/j.febslet.2004.07.079</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2004-08, Vol.573 (1), p.121-126 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_66816512 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; ScienceDirect Journals (5 years ago - present); Wiley Online Library All Journals; Alma/SFX Local Collection |
| subjects | Acids - chemistry Acids - metabolism Amino Acid Sequence Animals Binding Sites Ca 2+-induced extrusion Ca2+-induced extrusion Calcineurin Calcineurin - chemistry Calcineurin - metabolism Calcium - metabolism Calcium - pharmacology Calmodulin Calmodulin - metabolism Models, Molecular Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Binding Protein Structure, Tertiary Rats Small-angle X-ray scattering Static Electricity Substrate Specificity X-Ray Diffraction |
| title | Target recognition by calmodulin: the role of acid region contiguous to the calmodulin-binding domain of calcineurin A |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-11T23%3A45%3A34IST&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=Target%20recognition%20by%20calmodulin:%20the%20role%20of%20acid%20region%20contiguous%20to%20the%20calmodulin-binding%20domain%20of%20calcineurin%20A&rft.jtitle=FEBS%20letters&rft.au=Noguchi,%20Masahiro&rft.date=2004-08-27&rft.volume=573&rft.issue=1&rft.spage=121&rft.epage=126&rft.pages=121-126&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/j.febslet.2004.07.079&rft_dat=%3Cproquest_cross%3E19715975%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=19715975&rft_id=info:pmid/15327986&rft_els_id=S0014579304009536&rfr_iscdi=true |