Thrombin: Structure and Function by Wolfram Bode, Robert Huber, Timothy J. Rydel, Alexander

By Wolfram Bode, Robert Huber, Timothy J. Rydel, Alexander Tulinsky (auth.), Lawrence J. Berliner (eds.)

Research on thrombin constitution and serve as has stepped forward considerably during the last 3 many years. we're constantly researching new services f()r this enzyme in biology. but, till particularly lately, an entire, unique, 3­ dimensional photograph of its constitution used to be tricky to realize. We think that this article represents a turning aspect and, extra accurately, a brand new begin­ ing aspect for thrombin reports. Our target for this article is to provide an intensive and rounded-out assurance of thrombin chemistry and biochem­ istry so as to give you the biochemist and physiologist with a superb table reference on nearly any thrombin-related challenge. This quantity is equipped into 3 basic thrombin subject components: constitution, Biochemistry, and body structure. partially 1, constitution, we open with the full 3-dimensional x-ray constructions of 2 inhibited human thrombin complexes, one in every of that's the thrombin-hirudin com­ plex. those complexes also are addressed within the bankruptcy on structural reports in answer, which come with NMR, ESR, and fluorescence. half 2, Biochemistry, contains chapters on man made thrombin inhibitors, protein inhibitors (e.g., antithrombin III, hirudin), and thrombin interactions with issue XIII. half three, body structure, covers such issues as chemotactic actions, interactions with telephone surfaces, and the vascular endothelium.

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The hirudin tail interaction, Fig. 20). Due to its interaction with various anionic compounds and protein segments, this exosite is usually referred to as "anion-binding exosite" (Fenton, 1986). This could, however, lead to confusion with respect to the putative "heparin-binding site" described below. A more appropriate designation seems to be the term "fibrin(ogen)-recognizing exosite" (Fenton, 1981), due to the importance of this exosite in fibrinogen clotting and fibrin binding. The exposed peptide bond Arg-77A-Asn-78, in the 70-80 loop (Fig.

Hirudin segment Ile-l'-Thr-4' (thick connections) and surrounding residues of thrombin (thin connections) displayed together with the Connolly surface of the thrombin component and localized solvent molecules (crosses). The surface "hole" (lower left) marks the entrance to the specificity pocket. The amino-terminal hirudin segment runs parallel to thrombin segment 5er-2l4-Gly-219; hirudin residue lie-I' occupies the hydrophobic cavitylike 52 subsite of thrombin; its amino group is in hydrogen bond distance of 5er-195 OG.

1992). , 1979) and accelerates its inactivation by antithrombin III (Bjork and Lindahl, 1982). Chemical modification experiments on thrombin revealed that Lys169 and Lys-240 (at the edges of this positively charged patch, Fig. 10) are blocked by thrombin-bound heparin, and that their modification renders 28 WOLFRAM BODE et ai. Figure 10. Putative heparin-binding site of thrombin. The view is approximately toward the "top" of the thrombin molecule (compared with Fig. 5). Main-chain segments and all basic side chains in this surface area are emphasized by thick connections.

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