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1ixa

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(New page: 200px<br /> <applet load="1ixa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ixa" /> '''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRS...)
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[[Image:1ixa.gif|left|200px]]<br />
 
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<applet load="1ixa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ixa" />
 
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'''THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A'''<br />
 
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==Overview==
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==THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A==
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The three-dimensional structure of the first epidermal growth factor, (EGF)-like module from human factor IX has been determined in solution, using two-dimensional nuclear magnetic resonance (in the absence of, calcium and at pH 4.5). The structure was found to resemble closely that, of EGF and the homologous transforming growth factor-alpha (TGF-alpha)., Residues 60-65 form an antiparallel beta-sheet with residues 68-73. In the, C-terminal subdomain a type II beta-turn is found between residues 74 and, 77 and a five-residue turn is found between residues 79 and 83. Glu 78 and, Leu 84 pair in an antiparallel beta-sheet conformation. In the N-terminal, region a loop is found between residues 50 and 55 such that the side, chains of both are positioned above the face of the beta-sheet. Residues, 56-60 form a turn that leads into the first strand of the beta-sheet., Whereas the global fold closely resembles that of EGF, the N-terminal, residues of the module (46-49) do not form a beta-strand but are, ill-defined in the structure, probably due to the local flexibility of, this region. The structure is discussed with reference to recent, site-directed mutagenesis data, which have identified certain conserved, residues as ligands for calcium.
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<StructureSection load='1ixa' size='340' side='right'caption='[[1ixa]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ixa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IXA FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ixa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ixa OCA], [https://pdbe.org/1ixa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ixa RCSB], [https://www.ebi.ac.uk/pdbsum/1ixa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ixa ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN] Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:[https://omim.org/entry/306900 306900]; also known as Christmas disease.<ref>PMID:8295821</ref> <ref>PMID:2592373</ref> <ref>PMID:2743975</ref> <ref>PMID:6603618</ref> <ref>PMID:3009023</ref> <ref>PMID:3790720</ref> <ref>PMID:3401602</ref> <ref>PMID:3243764</ref> <ref>PMID:2713493</ref> <ref>PMID:2714791</ref> <ref>PMID:2773937</ref> <ref>PMID:2775660</ref> <ref>PMID:2753873</ref> <ref>PMID:2738071</ref> <ref>PMID:2472424</ref> <ref>PMID:2339358</ref> <ref>PMID:2372509</ref> <ref>PMID:2162822</ref> <ref>PMID:1958666</ref> <ref>PMID:1902289</ref> <ref>PMID:1346975</ref> <ref>PMID:1615485</ref> <ref>PMID:8257988</ref> <ref>PMID:8076946</ref> <ref>PMID:8199596</ref> <ref>PMID:7981722</ref> <ref>PMID:8680410</ref> <ref>PMID:9222764</ref> <ref>PMID:9590153</ref> <ref>PMID:9452115</ref> <ref>PMID:9600455</ref> <ref>PMID:10698280</ref> <ref>PMID:10094553</ref> <ref>PMID:11122099</ref> <ref>PMID:12588353</ref> <ref>PMID:12604421</ref> Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide. Defects in F9 are the cause of thrombophilia due to factor IX defect (THPH8) [MIM:[https://omim.org/entry/300807 300807]. A hemostatic disorder characterized by a tendency to thrombosis.<ref>PMID:19846852</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/FA9_HUMAN FA9_HUMAN] Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ix/1ixa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ixa ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Hemophilia B OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=306900 306900]], Warfarin sensitivity OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=306900 306900]]
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*[[Factor IX 3D structures|Factor IX 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1IXA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IXA OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha., Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AG, Brownlee GG, Campbell ID, Protein Sci. 1992 Jan;1(1):81-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1304885 1304885]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Baron, M.]]
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[[Category: Baron M]]
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[[Category: Brownlee, G.G.]]
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[[Category: Brownlee GG]]
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[[Category: Campbell, I.D.C.]]
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[[Category: Campbell IDC]]
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[[Category: Hanford, P.A.]]
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[[Category: Hanford PA]]
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[[Category: Harvey, T.S.]]
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[[Category: Harvey TS]]
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[[Category: Mayhew, M.]]
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[[Category: Mayhew M]]
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[[Category: Norman, D.G.]]
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[[Category: Norman DG]]
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[[Category: Tse, A.G.D.]]
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[[Category: Tse AGD]]
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[[Category: human factor ix]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:35:39 2007''
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Current revision

THE THREE-DIMENSIONAL STRUCTURE OF THE FIRST EGF-LIKE MODULE OF HUMAN FACTOR IX: COMPARISON WITH EGF AND TGF-A

PDB ID 1ixa

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