3tgi
From Proteopedia
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[[Category: complex (serine protease/inhibitor)]] | [[Category: complex (serine protease/inhibitor)]] | ||
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Revision as of 15:42, 30 October 2007
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WILD-TYPE RAT ANIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)
Overview
Unlike bovine cationic trypsin, rat anionic trypsin retains activity at, high pH. This alkaline stability has been attributed to stabilization of, the salt bridge between the N-terminal Ile16 and Asp194 by the surface, negative charge (Soman K, Yang A-S, Honig B, Fletterick R., 1989, Biochemistry 28:9918-9926). The formation of this salt bridge controls the, conformation of the activation domain in trypsin. In this work we probe, the structure of rat trypsinogen to determine the effects of the surface, negative charge on the activation domain in the absence of the, Ile16-Asp194 salt bridge. We determined the crystal structures of the rat, trypsin-BPTI complex and the rat trypsinogen-BPTI complex at 1.8 and 2.2, A, respectively. The BPTI complex of rat trypsinogen resembles that of rat, ... [(full description)]
About this Structure
3TGI is a [Protein complex] structure of sequences from [Bos taurus] and [Rattus norvegicus] with CA and SO4 as [ligands]. Active as [Trypsin], with EC number [3.4.21.4]. Structure known Active Sites: CAT and P1. Full crystallographic information is available from [OCA].
Reference
Comparison of anionic and cationic trypsinogens: the anionic activation domain is more flexible in solution and differs in its mode of BPTI binding in the crystal structure., Pasternak A, Ringe D, Hedstrom L, Protein Sci. 1999 Jan;8(1):253-8. PMID:10210204
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