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1jy3

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Revision as of 06:47, 11 August 2021

Crystal Structure of the Central Region of Bovine Fibrinogen (E5 Fragment) at 1.4 Angstroms Resolution

Structural highlights

1jy3 is a 6 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1jy2
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FIBG_BOVIN] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. [FIBB_BOVIN] 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 PubMed

The high-resolution crystal structure of the N-terminal central region of bovine fibrinogen (a 35-kDa E(5) fragment) reveals a remarkable dimeric design. The two halves of the molecule bond together at the center in an extensive molecular "handshake" by using both disulfide linkages and noncovalent contacts. On one face of the fragment, the Aalpha and Bbeta chains from the two monomers form a funnel-shaped domain with an unusual hydrophobic cavity; here, on each of the two outer sides there appears to be a binding site for thrombin. On the opposite face, the N-terminal gamma chains fold into a separate domain. Despite the chemical identity of the two halves of fibrinogen, an unusual pair of adjacent disulfide bonds locally constrain the two gamma chains to adopt different conformations. The striking asymmetry of this domain may promote the known supercoiling of the protofibrils in fibrin. This information on the detailed topology of the E(5) fragment permits the construction of a more detailed model than previously possible for the critical trimolecular junction of the protofibril in fibrin.

Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution.,Madrazo J, Brown JH, Litvinovich S, Dominguez R, Yakovlev S, Medved L, Cohen C Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11967-72. PMID:11593005^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Madrazo J, Brown JH, Litvinovich S, Dominguez R, Yakovlev S, Medved L, Cohen C. Crystal structure of the central region of bovine fibrinogen (E5 fragment) at 1.4-A resolution. Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11967-72. PMID:11593005 doi:10.1073/pnas.211439798

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jy3"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jy3' size='340' side='right'caption='[[1jy3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jy3]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JY3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jy3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JY3 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jy2|1jy2]]</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;'>[[1jy2|1jy2]]</div></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=1jy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jy3 OCA], [http://pdbe.org/1jy3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jy3 RCSB], [http://www.ebi.ac.uk/pdbsum/1jy3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jy3 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=1jy3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jy3 OCA], [https://pdbe.org/1jy3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jy3 RCSB], [https://www.ebi.ac.uk/pdbsum/1jy3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jy3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FIBG_BOVIN FIBG_BOVIN]] 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_BOVIN FIBB_BOVIN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
+[[https://www.uniprot.org/uniprot/FIBG_BOVIN FIBG_BOVIN]] 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_BOVIN FIBB_BOVIN]] 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]]

1jy3

From Proteopedia

Revision as of 06:47, 11 August 2021

Crystal Structure of the Central Region of Bovine Fibrinogen (E5 Fragment) at 1.4 Angstroms Resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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