1ei3: Difference between revisions

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 ==CRYSTAL STRUCTURE OF NATIVE CHICKEN FIBRINOGEN==
-<StructureSection load='1ei3' size='340' side='right' caption='[[1ei3]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
+<StructureSection load='1ei3' size='340' side='right'caption='[[1ei3]], [[Resolution|resolution]] 5.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ei3]] is a 6 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EI3 FirstGlance]. <br>
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 5.5&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ei3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ei3 OCA], [http://pdbe.org/1ei3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ei3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ei3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ei3 ProSAT]</span></td></tr>
+<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>
 == Function ==
-[[http://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. [[http://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.
+[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </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=1ei3 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The 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<ref>PMID:10737772</ref>
+==See Also==
+*[[Fibrinogen|Fibrinogen]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1ei3" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Doolittle, R F]]
+[[Category: Large Structures]]
-[[Category: Mochalkin, I]]
+[[Category: Doolittle RF]]
-[[Category: Riley, M]]
+[[Category: Mochalkin I]]
-[[Category: Veerapandian, L]]
+[[Category: Riley M]]
-[[Category: Yang, Z]]
+[[Category: Veerapandian L]]
-[[Category: Blood clotting]]
+[[Category: Yang Z]]
-[[Category: Coiled coil]]
-[[Category: Disulfide ring]]
-[[Category: Fibrin forming entity]]