The first EGF‐like domain from human factor IX contains a high‐affinity calcium binding site
It has been suggested that epidermal growth factor‐like (EGF‐like) domains, containing conserved carboxylate residues, are responsible for the high‐affinity calcium binding exhibited by a number of vitamin K‐dependent plasma proteins involved in the control of the blood coagulation cascade. These in...
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| Veröffentlicht in: | The EMBO journal 1990-02, Vol.9 (2), p.475-480 |
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| creator | Handford, P.A. Baron, M. Mayhew, M. Willis, A. Beesley, T. Brownlee, G.G. Campbell, I.D. |
| description | It has been suggested that epidermal growth factor‐like (EGF‐like) domains, containing conserved carboxylate residues, are responsible for the high‐affinity calcium binding exhibited by a number of vitamin K‐dependent plasma proteins involved in the control of the blood coagulation cascade. These include the procoagulant factors IX and X, and the anticoagulants protein C and protein S. To test this hypothesis we have expressed the first EGF‐like domain from human factor IX (residues 46‐84) using a yeast secretion system, and examined calcium binding to the domain. Using 1H‐NMR to measure a calcium‐dependent shift assigned to Tyr69 we have detected a high‐affinity calcium binding site (Kd = 200‐300 microM). We suggest that other EGF‐like domains of this type may have similar calcium binding properties. In addition, we have completely assigned the aromatic region of the NMR spectrum by NOESY and COSY analysis, and have used these data to discuss the effect of calcium and pH on the conformation of the domain with reference to a model based on the structure of human EGF. |
| doi_str_mv | 10.1002/j.1460-2075.1990.tb08133.x |
| format | Article |
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These include the procoagulant factors IX and X, and the anticoagulants protein C and protein S. To test this hypothesis we have expressed the first EGF‐like domain from human factor IX (residues 46‐84) using a yeast secretion system, and examined calcium binding to the domain. Using 1H‐NMR to measure a calcium‐dependent shift assigned to Tyr69 we have detected a high‐affinity calcium binding site (Kd = 200‐300 microM). We suggest that other EGF‐like domains of this type may have similar calcium binding properties. In addition, we have completely assigned the aromatic region of the NMR spectrum by NOESY and COSY analysis, and have used these data to discuss the effect of calcium and pH on the conformation of the domain with reference to a model based on the structure of human EGF.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1002/j.1460-2075.1990.tb08133.x</identifier><identifier>PMID: 2406129</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>London: Nature Publishing Group</publisher><subject>Amino Acid Sequence ; Base Sequence ; Binding Sites ; Biological and medical sciences ; Blood coagulation. Blood cells ; Calcium - metabolism ; Cloning, Molecular ; Disulfides - analysis ; Epidermal Growth Factor - genetics ; Factor IX - genetics ; Factor IX - metabolism ; Fundamental and applied biological sciences. Psychology ; General aspects, investigation methods, hemostasis, fibrinolysis ; Genetic Vectors ; Humans ; Magnetic Resonance Spectroscopy ; Molecular and cellular biology ; Molecular Sequence Data ; Oligonucleotide Probes ; Protein Conformation ; Restriction Mapping ; Saccharomyces cerevisiae - genetics ; Sequence Homology, Nucleic Acid</subject><ispartof>The EMBO journal, 1990-02, Vol.9 (2), p.475-480</ispartof><rights>1990 European Molecular Biology Organization</rights><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5733-d084edd9e2484b9807d91f15d24769a9e5c6edc42c5124b62c34f5bd90b75cab3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC551689/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC551689/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27903,27904,53769,53771</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6809661$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2406129$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Handford, P.A.</creatorcontrib><creatorcontrib>Baron, M.</creatorcontrib><creatorcontrib>Mayhew, M.</creatorcontrib><creatorcontrib>Willis, A.</creatorcontrib><creatorcontrib>Beesley, T.</creatorcontrib><creatorcontrib>Brownlee, G.G.</creatorcontrib><creatorcontrib>Campbell, I.D.</creatorcontrib><title>The first EGF‐like domain from human factor IX contains a high‐affinity calcium binding site</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><description>It has been suggested that epidermal growth factor‐like (EGF‐like) domains, containing conserved carboxylate residues, are responsible for the high‐affinity calcium binding exhibited by a number of vitamin K‐dependent plasma proteins involved in the control of the blood coagulation cascade. These include the procoagulant factors IX and X, and the anticoagulants protein C and protein S. To test this hypothesis we have expressed the first EGF‐like domain from human factor IX (residues 46‐84) using a yeast secretion system, and examined calcium binding to the domain. Using 1H‐NMR to measure a calcium‐dependent shift assigned to Tyr69 we have detected a high‐affinity calcium binding site (Kd = 200‐300 microM). We suggest that other EGF‐like domains of this type may have similar calcium binding properties. In addition, we have completely assigned the aromatic region of the NMR spectrum by NOESY and COSY analysis, and have used these data to discuss the effect of calcium and pH on the conformation of the domain with reference to a model based on the structure of human EGF.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Binding Sites</subject><subject>Biological and medical sciences</subject><subject>Blood coagulation. Blood cells</subject><subject>Calcium - metabolism</subject><subject>Cloning, Molecular</subject><subject>Disulfides - analysis</subject><subject>Epidermal Growth Factor - genetics</subject><subject>Factor IX - genetics</subject><subject>Factor IX - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>General aspects, investigation methods, hemostasis, fibrinolysis</subject><subject>Genetic Vectors</subject><subject>Humans</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Oligonucleotide Probes</subject><subject>Protein Conformation</subject><subject>Restriction Mapping</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkc1u1DAUhS0EKkPhEZAshNgltR3_xEgsSjX9Uys2RWJnHMeeeEicYifQ2fEIPCNPQsJEI1iy8pXOOddH9wPgFUY5RoicbHNMOcoIEizHUqJ8qFCJiyJ_eARWB-kxWCHCcUZxKZ-CZyltEUKsFPgIHBGKOCZyBT7fNRY6H9MA1xfnv378bP0XC-u-0z5AF_sONmOnp1GboY_w6hM0fRgmMUENG79ppoh2zgc_7KDRrfFjBysfah82MPnBPgdPnG6TfbG8x-Dj-fru7DK7-XBxdXZ6kxkmiiKrUUltXUtLaEkrWSJRS-wwqwkVXGppmeG2NpQYhgmtODEFdayqJaoEM7oqjsG7_d77seompw1D1K26j77Tcad67dW_SvCN2vTfFGOYl3LKv1nysf862jSozidj21YH249JCcmxEBRPxrd7o4l9StG6wx8YqRmP2qqZgZoZqBmPWvCohyn88u-Wh-jCY9JfL7pO0zVd1MH4dLDxEknO5w6ne9t339rdfxRQ69v313_m4jd7LbCP</recordid><startdate>199002</startdate><enddate>199002</enddate><creator>Handford, P.A.</creator><creator>Baron, M.</creator><creator>Mayhew, M.</creator><creator>Willis, A.</creator><creator>Beesley, T.</creator><creator>Brownlee, G.G.</creator><creator>Campbell, I.D.</creator><general>Nature Publishing Group</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>7X8</scope><scope>5PM</scope></search><sort><creationdate>199002</creationdate><title>The first EGF‐like domain from human factor IX contains a high‐affinity calcium binding site</title><author>Handford, P.A. ; Baron, M. ; Mayhew, M. ; Willis, A. ; Beesley, T. ; Brownlee, G.G. ; Campbell, I.D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5733-d084edd9e2484b9807d91f15d24769a9e5c6edc42c5124b62c34f5bd90b75cab3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Biological and medical sciences</topic><topic>Blood coagulation. Blood cells</topic><topic>Calcium - metabolism</topic><topic>Cloning, Molecular</topic><topic>Disulfides - analysis</topic><topic>Epidermal Growth Factor - genetics</topic><topic>Factor IX - genetics</topic><topic>Factor IX - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>General aspects, investigation methods, hemostasis, fibrinolysis</topic><topic>Genetic Vectors</topic><topic>Humans</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Oligonucleotide Probes</topic><topic>Protein Conformation</topic><topic>Restriction Mapping</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Handford, P.A.</creatorcontrib><creatorcontrib>Baron, M.</creatorcontrib><creatorcontrib>Mayhew, M.</creatorcontrib><creatorcontrib>Willis, A.</creatorcontrib><creatorcontrib>Beesley, T.</creatorcontrib><creatorcontrib>Brownlee, G.G.</creatorcontrib><creatorcontrib>Campbell, I.D.</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Handford, P.A.</au><au>Baron, M.</au><au>Mayhew, M.</au><au>Willis, A.</au><au>Beesley, T.</au><au>Brownlee, G.G.</au><au>Campbell, I.D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The first EGF‐like domain from human factor IX contains a high‐affinity calcium binding site</atitle><jtitle>The EMBO journal</jtitle><addtitle>EMBO J</addtitle><date>1990-02</date><risdate>1990</risdate><volume>9</volume><issue>2</issue><spage>475</spage><epage>480</epage><pages>475-480</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>It has been suggested that epidermal growth factor‐like (EGF‐like) domains, containing conserved carboxylate residues, are responsible for the high‐affinity calcium binding exhibited by a number of vitamin K‐dependent plasma proteins involved in the control of the blood coagulation cascade. These include the procoagulant factors IX and X, and the anticoagulants protein C and protein S. To test this hypothesis we have expressed the first EGF‐like domain from human factor IX (residues 46‐84) using a yeast secretion system, and examined calcium binding to the domain. Using 1H‐NMR to measure a calcium‐dependent shift assigned to Tyr69 we have detected a high‐affinity calcium binding site (Kd = 200‐300 microM). We suggest that other EGF‐like domains of this type may have similar calcium binding properties. In addition, we have completely assigned the aromatic region of the NMR spectrum by NOESY and COSY analysis, and have used these data to discuss the effect of calcium and pH on the conformation of the domain with reference to a model based on the structure of human EGF.</abstract><cop>London</cop><pub>Nature Publishing Group</pub><pmid>2406129</pmid><doi>10.1002/j.1460-2075.1990.tb08133.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Base Sequence Binding Sites Biological and medical sciences Blood coagulation. Blood cells Calcium - metabolism Cloning, Molecular Disulfides - analysis Epidermal Growth Factor - genetics Factor IX - genetics Factor IX - metabolism Fundamental and applied biological sciences. Psychology General aspects, investigation methods, hemostasis, fibrinolysis Genetic Vectors Humans Magnetic Resonance Spectroscopy Molecular and cellular biology Molecular Sequence Data Oligonucleotide Probes Protein Conformation Restriction Mapping Saccharomyces cerevisiae - genetics Sequence Homology, Nucleic Acid |
| title | The first EGF‐like domain from human factor IX contains a high‐affinity calcium binding site |
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