1ei3: Difference between revisions
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<StructureSection load='1ei3' size='340' side='right'caption='[[1ei3]], [[Resolution|resolution]] 5.50Å' scene=''> | <StructureSection load='1ei3' size='340' side='right'caption='[[1ei3]], [[Resolution|resolution]] 5.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ei3]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ei3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EI3 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fzc|1fzc]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fzc|1fzc]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ei3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei3 OCA], [https://pdbe.org/1ei3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ei3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ei3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/FIBA_CHICK FIBA_CHICK]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. [[https://www.uniprot.org/uniprot/FIBB_CHICK FIBB_CHICK]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 12:37, 21 July 2021
CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGENCRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN
Structural highlights
Function[FIBA_CHICK] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. [FIBB_CHICK] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of native chicken fibrinogen has been determined at a resolution of 5.5 A. The full-length molecule is 460 A in length and sigmoidally shaped. The structure includes the full sweep of the coiled coils that connect the central and terminal domains; the chain paths of the central domain confirm a predicted scheme of planar disulfide rings in apposition with each other. Electron density maps have revealed the outlines of disordered alphaC domains nestled within the confines of the sinuous coiled coils. The amino-terminal segments of the alpha- and beta-chains, including the fibrinopeptides A and B, are also disordered. Crystal structure of native chicken fibrinogen at 5.5-A resolution.,Yang Z, Mochalkin I, Veerapandian L, Riley M, Doolittle RF Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3907-12. PMID:10737772[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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