1fid

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spinqualitylabelsall models 1fid, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF HUMAN GAMMA FIBRINOGEN 30 KD CARBOXYL TERMINAL FRAGMENT

Overview

BACKGROUND: 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., RESULTS: The ... [(full description)]

About this Structure

1FID is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Site: CAB. Full crystallographic information is available from [OCA].

Reference

Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen., Yee VC, Pratt KP, Cote HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC, Structure. 1997 Jan 15;5(1):125-38. PMID:9016719

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