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1fid

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(New page: 200px<br /> <applet load="1fid" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fid, resolution 2.1&Aring;" /> '''STRUCTURE OF HUMAN G...)
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[[Image:1fid.gif|left|200px]]<br />
 
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<applet load="1fid" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fid, resolution 2.1&Aring;" />
 
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'''STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT'''<br />
 
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==Overview==
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==STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT==
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BACKGROUND: Blood coagulation occurs by a cascade of zymogen activation, resulting from minor proteolysis. The final stage of coagulation involves, thrombin generation and limited proteolysis of fibrinogen to give, spontaneously polymerizing fibrin. The resulting fibrin network is, covalently crosslinked by factor XIIIa to yield a stable blood clot., Fibrinogen is a 340 kDa glycoprotein composed of six polypeptide chains, (alphabetagamma)2, held together by 29 disulfide bonds. The globular C, terminus of the gamma chain contains a fibrin-polymerization surface, the, principal factor XIIIa crosslinking site, the platelet receptor, recognition site, and a calcium-binding site. Structural information on, this domain should thus prove helpful in understanding clot formation., RESULTS: The ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9016719 (full description)]]
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<StructureSection load='1fid' size='340' side='right'caption='[[1fid]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FID 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">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</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=CA:CALCIUM+ION'>CA</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=1fid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fid OCA], [https://pdbe.org/1fid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fid RCSB], [https://www.ebi.ac.uk/pdbsum/1fid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fid ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN] Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:[https://omim.org/entry/202400 202400]. This rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=Patients with congenital fibrinogen abnormalities can manifest different clinical pictures. Some cases are clinically silent, some show a tendency toward bleeding and some show a predisposition for thrombosis with or without bleeding.
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== Function ==
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[https://www.uniprot.org/uniprot/FIBG_HUMAN FIBG_HUMAN] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
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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/fi/1fid_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=1fid ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1FID 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 CA as [[http://en.wikipedia.org/wiki/ligand ligand]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FID OCA]].
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*[[Fibrinogen|Fibrinogen]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen., Yee VC, Pratt KP, Cote HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC, Structure. 1997 Jan 15;5(1):125-38. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9016719 9016719]
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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: Teller, D.C.]]
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[[Category: Teller DC]]
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[[Category: Yee, V.C.]]
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[[Category: Yee VC]]
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[[Category: CA]]
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[[Category: alternative splicing]]
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[[Category: blood coagulation]]
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[[Category: calcium]]
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[[Category: disease mutation]]
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[[Category: glycoprotein]]
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[[Category: plasma]]
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[[Category: platelet]]
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[[Category: polymorphism]]
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[[Category: signal]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 22:14:42 2007''
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Current revision

STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

PDB ID 1fid

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