Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin

被引:378
作者
Spraggon, G [1 ]
Everse, SJ [1 ]
Doolittle, RF [1 ]
机构
[1] UNIV CALIF SAN DIEGO, CTR MOL GENET, LA JOLLA, CA 92093 USA
关键词
D O I
10.1038/38947
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
In blood coagulation, units of the protein fibrinogen pack together to form a fibrin clot, but a crystal structure for fibrinogen is needed to understand how this is achieved. The structure of a cove fragment (fragment D) from human fibrinogen has now been determined to 2.9 Angstrom resolution. The 86K three-chained structure consists of a coiled-coil region and two homologous globular entities oriented at approximately 130 degrees to each other, Additionally, the covalently bound dimer of fragment D, known as 'doubte-D', was isolated from human fibrin, crystallized in the presence of a Gly-Pro-Arg-Pro-amide peptide ligand, which simulates the donor polymerization site, and its structure solved by molecular replacement with the model of fragment D.
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页码:455 / 462
页数:8
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