Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties
Equine platelet β tropomyosin (247 residues), like rabbit skeletal muscle α tropomyosin (284 residues) has a repeating pattern of amino acid residues characterisitic of a coiled-coil structure. When compared with the muscle protein, it is extended by 5 residues at the NH 2-terminus and possesses two...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 1983-06, Vol.156 (2), p.269-273 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 273 |
|---|---|
| container_issue | 2 |
| container_start_page | 269 |
| container_title | FEBS letters |
| container_volume | 156 |
| creator | Lewis, William G. Cote, Graham P. Mak, Alan S. Smillie, Lawrence B. |
| description | Equine platelet β tropomyosin (247 residues), like rabbit skeletal muscle α tropomyosin (284 residues) has a repeating pattern of amino acid residues characterisitic of a coiled-coil structure. When compared with the muscle protein, it is extended by 5 residues at the NH
2-terminus and possesses two 21 residue deletions (positions 23–43 and 60–80 of the muscle sequence). The two proteins are highly conserved from residues 81–260, but are significantly different at their COOH-termini (residues 261–284). These differences in platelet tropomyosin can be correlated with its diminshed head-to-tail polymerization, a weaker interaction with F-actin and a reduced affinity for muscle troponin and the T1 fragment of troponin-T. |
| doi_str_mv | 10.1016/0014-5793(83)80511-0 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_80486938</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0014579383805110</els_id><sourcerecordid>80486938</sourcerecordid><originalsourceid>FETCH-LOGICAL-c337t-8bf4008f014a41efc3627ce34aa9398452346c6892543bab32e0b37ac03eafc53</originalsourceid><addsrcrecordid>eNqFkE1LxDAQhoMo67r6DxRyEj1UkyZtUw_CsvgFC1705CGk6RQjbVOTrLL_3tRd9qgQmGTed2YyD0KnlFxRQvNrQihPsqJkF4JdCpJRmpA9NKWiYAnjudhH053lEB15_0HiW9Bygia5yNI0J1P0Nu9Mb7HSpsYePlfQa8C2wfFqesBDqwK0EHBwdrDd2nrT3-CFdQ6iYmyPv014x6YP4JT-TQzRCS4Y8MfooFGth5NtnKHX-7uXxWOyfH54WsyXiWasCImoGk6IaOJfFafQaJanhQbGlSpZKXiWxm10Lso046xSFUuBVKxQmjBQjc7YDJ1v-sbRcQMfZGe8hrZVPdiVl4JwkZdM_GukLM9oVvBo5BujdtZ7B40cnOmUW0tK5AhfjmTlSFaKeEb4ksSys23_VdVBvSva0o767UaHSOPLgJNem5F4bRzoIGtr_h7wAzFSlCw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>13651574</pqid></control><display><type>article</type><title>Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals Complete</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Lewis, William G. ; Cote, Graham P. ; Mak, Alan S. ; Smillie, Lawrence B.</creator><creatorcontrib>Lewis, William G. ; Cote, Graham P. ; Mak, Alan S. ; Smillie, Lawrence B.</creatorcontrib><description>Equine platelet β tropomyosin (247 residues), like rabbit skeletal muscle α tropomyosin (284 residues) has a repeating pattern of amino acid residues characterisitic of a coiled-coil structure. When compared with the muscle protein, it is extended by 5 residues at the NH
2-terminus and possesses two 21 residue deletions (positions 23–43 and 60–80 of the muscle sequence). The two proteins are highly conserved from residues 81–260, but are significantly different at their COOH-termini (residues 261–284). These differences in platelet tropomyosin can be correlated with its diminshed head-to-tail polymerization, a weaker interaction with F-actin and a reduced affinity for muscle troponin and the T1 fragment of troponin-T.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(83)80511-0</identifier><identifier>PMID: 6852260</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Animals ; Blood Platelets - metabolism ; Chemical Phenomena ; Chemistry ; Coiled-coil Contractile protein Actin-binding Troponin interaction Non-muscle Ca 2+ regulation ; horses ; Horses - blood ; Muscles - analysis ; platelets ; Protein Binding ; Rabbits ; Species Specificity ; tropomyosin ; Tropomyosin - blood</subject><ispartof>FEBS letters, 1983-06, Vol.156 (2), p.269-273</ispartof><rights>1983</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c337t-8bf4008f014a41efc3627ce34aa9398452346c6892543bab32e0b37ac03eafc53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(83)80511-0$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6852260$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lewis, William G.</creatorcontrib><creatorcontrib>Cote, Graham P.</creatorcontrib><creatorcontrib>Mak, Alan S.</creatorcontrib><creatorcontrib>Smillie, Lawrence B.</creatorcontrib><title>Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Equine platelet β tropomyosin (247 residues), like rabbit skeletal muscle α tropomyosin (284 residues) has a repeating pattern of amino acid residues characterisitic of a coiled-coil structure. When compared with the muscle protein, it is extended by 5 residues at the NH
2-terminus and possesses two 21 residue deletions (positions 23–43 and 60–80 of the muscle sequence). The two proteins are highly conserved from residues 81–260, but are significantly different at their COOH-termini (residues 261–284). These differences in platelet tropomyosin can be correlated with its diminshed head-to-tail polymerization, a weaker interaction with F-actin and a reduced affinity for muscle troponin and the T1 fragment of troponin-T.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Blood Platelets - metabolism</subject><subject>Chemical Phenomena</subject><subject>Chemistry</subject><subject>Coiled-coil Contractile protein Actin-binding Troponin interaction Non-muscle Ca 2+ regulation</subject><subject>horses</subject><subject>Horses - blood</subject><subject>Muscles - analysis</subject><subject>platelets</subject><subject>Protein Binding</subject><subject>Rabbits</subject><subject>Species Specificity</subject><subject>tropomyosin</subject><subject>Tropomyosin - blood</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1LxDAQhoMo67r6DxRyEj1UkyZtUw_CsvgFC1705CGk6RQjbVOTrLL_3tRd9qgQmGTed2YyD0KnlFxRQvNrQihPsqJkF4JdCpJRmpA9NKWiYAnjudhH053lEB15_0HiW9Bygia5yNI0J1P0Nu9Mb7HSpsYePlfQa8C2wfFqesBDqwK0EHBwdrDd2nrT3-CFdQ6iYmyPv014x6YP4JT-TQzRCS4Y8MfooFGth5NtnKHX-7uXxWOyfH54WsyXiWasCImoGk6IaOJfFafQaJanhQbGlSpZKXiWxm10Lso046xSFUuBVKxQmjBQjc7YDJ1v-sbRcQMfZGe8hrZVPdiVl4JwkZdM_GukLM9oVvBo5BujdtZ7B40cnOmUW0tK5AhfjmTlSFaKeEb4ksSys23_VdVBvSva0o767UaHSOPLgJNem5F4bRzoIGtr_h7wAzFSlCw</recordid><startdate>19830613</startdate><enddate>19830613</enddate><creator>Lewis, William G.</creator><creator>Cote, Graham P.</creator><creator>Mak, Alan S.</creator><creator>Smillie, Lawrence B.</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19830613</creationdate><title>Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties</title><author>Lewis, William G. ; Cote, Graham P. ; Mak, Alan S. ; Smillie, Lawrence B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c337t-8bf4008f014a41efc3627ce34aa9398452346c6892543bab32e0b37ac03eafc53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Blood Platelets - metabolism</topic><topic>Chemical Phenomena</topic><topic>Chemistry</topic><topic>Coiled-coil Contractile protein Actin-binding Troponin interaction Non-muscle Ca 2+ regulation</topic><topic>horses</topic><topic>Horses - blood</topic><topic>Muscles - analysis</topic><topic>platelets</topic><topic>Protein Binding</topic><topic>Rabbits</topic><topic>Species Specificity</topic><topic>tropomyosin</topic><topic>Tropomyosin - blood</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lewis, William G.</creatorcontrib><creatorcontrib>Cote, Graham P.</creatorcontrib><creatorcontrib>Mak, Alan S.</creatorcontrib><creatorcontrib>Smillie, Lawrence B.</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lewis, William G.</au><au>Cote, Graham P.</au><au>Mak, Alan S.</au><au>Smillie, Lawrence B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1983-06-13</date><risdate>1983</risdate><volume>156</volume><issue>2</issue><spage>269</spage><epage>273</epage><pages>269-273</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Equine platelet β tropomyosin (247 residues), like rabbit skeletal muscle α tropomyosin (284 residues) has a repeating pattern of amino acid residues characterisitic of a coiled-coil structure. When compared with the muscle protein, it is extended by 5 residues at the NH
2-terminus and possesses two 21 residue deletions (positions 23–43 and 60–80 of the muscle sequence). The two proteins are highly conserved from residues 81–260, but are significantly different at their COOH-termini (residues 261–284). These differences in platelet tropomyosin can be correlated with its diminshed head-to-tail polymerization, a weaker interaction with F-actin and a reduced affinity for muscle troponin and the T1 fragment of troponin-T.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>6852260</pmid><doi>10.1016/0014-5793(83)80511-0</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 1983-06, Vol.156 (2), p.269-273 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80486938 |
| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Blood Platelets - metabolism Chemical Phenomena Chemistry Coiled-coil Contractile protein Actin-binding Troponin interaction Non-muscle Ca 2+ regulation horses Horses - blood Muscles - analysis platelets Protein Binding Rabbits Species Specificity tropomyosin Tropomyosin - blood |
| title | Amino acid sequence of equine platelet tropomyosin: Correlation with interaction properties |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T23%3A24%3A19IST&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=Amino%20acid%20sequence%20of%20equine%20platelet%20tropomyosin:%20Correlation%20with%20interaction%20properties&rft.jtitle=FEBS%20letters&rft.au=Lewis,%20William%20G.&rft.date=1983-06-13&rft.volume=156&rft.issue=2&rft.spage=269&rft.epage=273&rft.pages=269-273&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/0014-5793(83)80511-0&rft_dat=%3Cproquest_cross%3E80486938%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=13651574&rft_id=info:pmid/6852260&rft_els_id=0014579383805110&rfr_iscdi=true |