1FIC

STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

Summary for 1FIC

• Entry DOI: 10.2210/pdb1fic/pdb
• Descriptor: GAMMA FIBRINOGEN, CALCIUM ION (3 entities in total)
• Functional Keywords: blood coagulation, glycoprotein, calcium, platelet, plasma, alternative splicing, disease mutation, polymorphism, blood coagulation factor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02679
• Total number of polymer chains: 2
• Total formula weight: 60567.00

Authors

Yee, V.C.,Teller, D.C. (deposition date: 1996-08-24, release date: 1997-04-01, Last modification date: 2024-11-06)

Primary citation

Yee, V.C.,Pratt, K.P.,Cote, H.C.,Trong, I.L.,Chung, D.W.,Davie, E.W.,Stenkamp, R.E.,Teller, D.C.
Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen.
Structure, 5:125-138, 1997

PubMed Abstract: 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.

PubMed: 9016719
DOI: 10.1016/S0969-2126(97)00171-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)