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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yang Z, Mochalkin I, Veerapandian L, Riley M, Doolittle RF. Crystal structure of native chicken fibrinogen at 5.5-A resolution. Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3907-12. PMID:10737772 doi:10.1073/pnas.080065697
