期刊
BIOCHEMISTRY
卷 40, 期 42, 页码 12515-12523出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi011394p
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资金
- NHLBI NIH HHS [HL-26873] Funding Source: Medline
- NIGMS NIH HHS [GM 007240] Funding Source: Medline
The crystal structure of native chicken fibrinogen (320 kDa) complexed with two synthetic peptides has been determined at a resolution of 2.7 Angstrom. The structure provides the first atomic-resolution view of the polypeptide chain arrangement in the central domain where the two halves of the molecule are joined, as well as of a putative thrombin-binding site. The animo-terminal segments of the a and chains, including fibrinopeptides A and B, are not visible in electron density maps, however, and must be highly disordered. The alphaC domain is also very disordered. A residue by residue analysis of the coiled coils with regard to temperature factor shows a strong correlation between mobility and plasmin attack sites. It is concluded that structural flexibility is an inherent feature of fibrinogen that plays a key role in both its conversion to fibrin and its subsequent destruction by plasmin.
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