Bovine Thrombin Complexed with an Uncleavable Analog of Residues 7−19 of Fibrinogen Aα:  Geometry of the Catalytic Triad and Interactions of the P1‘, P2‘, and P3‘ Substrate Residues

The crystal structure of the noncovalent complex of bovine thrombin and a fibrinogen-Aα tridecapeptide substrate analog, G17ψ, in which the scissile bond amide nitrogen of Gly-17f has been replaced by a methylene carbon, has been determined at 2.3 Å resolution with an R factor of 17.1%. The geometry...

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Veröffentlicht in:	Biochemistry (Easton) 1996-10, Vol.35 (40), p.13030-13039
Hauptverfasser:	Martin, Philip D, Malkowski, Michael G, DiMaio, John, Konishi, Yasuo, Ni, Feng, Edwards, Brian F. P
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Cattle Crystallography, X-Ray Fibrinogen - chemistry Hirudins - analogs & derivatives Hirudins - chemistry Hydrogen Bonding Models, Molecular Peptide Fragments - chemistry Protein Conformation Thrombin - chemistry Thrombin - metabolism
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