1cfh

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(New page: 200px<br /> <applet load="1cfh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cfh" /> '''STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGL...)
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[[Image:1cfh.gif|left|200px]]<br />
 
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<applet load="1cfh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cfh" />
 
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'''STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY'''<br />
 
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==Overview==
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==STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY==
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The gamma-carboxyglutamic acid-rich domain of blood coagulation Factor IX, is required for the binding of the protein to phospholipid membranes. To, investigate the three-dimensional structure of this domain, a synthetic, peptide corresponding to residues 1-47 of Factor IX was studied by 1H NMR, spectroscopy. In the absence of metal ions, the proton chemical shift, dispersion in the one-dimensional NMR spectrum indicated that the peptide, contains regular structural elements. Upon the addition of Ca(II) or, Mg(II), large chemical shift changes were observed in the amide proton and, methyl proton regions of the spectrum, consistent with the conformational, transitions that metal ions are known to induce in native Factor IX. The, apopeptide was studied by two-dimensional NMR spectroscopy at 500 MHz to, determine its solution structure. Protons were assigned using total, correlation spectroscopy, nuclear Overhauser effect spectroscopy, and, double quantum-filtered correlation spectroscopy experiments. Intensities, of cross-peaks in the nuclear Overhauser effect spectrum were used to, generate a set of interproton distance restraints. The structure of the, apopeptide was then calculated using distance geometry methods. There are, three structural elements in the apopeptide that are linked by a flexible, polypeptide backbone. These elements include a short amino-terminal, tetrapeptide loop (amino acids 6-9), the disulfide-containing hexapeptide, loop (amino acids 18-23), and a carboxyl-terminal alpha helix (amino acids, 37-46). Amide hydrogen exchange kinetics indicate that the majority of the, peptide is solvent accessible, except in the carboxyl-terminal element., The structured regions in the apopeptide are insufficient to support, phospholipid binding, indicating the importance of additional structural, features in the Ca(II)-stabilized conformer.
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<StructureSection load='1cfh' size='340' side='right'caption='[[1cfh]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cfh]] 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=1CFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFH 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene></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=1cfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfh OCA], [https://pdbe.org/1cfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfh RCSB], [https://www.ebi.ac.uk/pdbsum/1cfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfh 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/cf/1cfh_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=1cfh 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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1CFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with FMT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CFH OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy., Freedman SJ, Furie BC, Furie B, Baleja JD, J Biol Chem. 1995 Apr 7;270(14):7980-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7713897 7713897]
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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: Baleja, J.D.]]
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[[Category: Baleja JD]]
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[[Category: Freedman, S.J.]]
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[[Category: Freedman SJ]]
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[[Category: Furie, B.]]
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[[Category: Furie B]]
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[[Category: Furie, B.C.]]
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[[Category: Furie BC]]
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[[Category: FMT]]
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[[Category: coagulation factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:21:22 2007''
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Current revision

STRUCTURE OF THE METAL-FREE GAMMA-CARBOXYGLUTAMIC ACID-RICH MEMBRANE BINDING REGION OF FACTOR IX BY TWO-DIMENSIONAL NMR SPECTROSCOPY

PDB ID 1cfh

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