8pch

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8pch, resolution 2.1Å

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CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION

Overview

BACKGROUND: Cathepsin H is a lysosomal cysteine protease, involved in, intracellular protein degradation. It is the only known, mono-aminopeptidase in the papain-like family and is reported to be, involved in tumor metastasis. The cathepsin H structure was determined in, order to investigate the structural basis for its aminopeptidase activity, and thus to provide the basis for structure-based design of synthetic, inhibitors. RESULTS: The crystal structure of native porcine cathepsin H, was determined at 2.1 A resolution. The structure has the typical, papain-family fold. The so-called mini-chain, the octapeptide EPQNCSAT, is, attached via a disulfide bond to the body of the enzyme and bound in a, narrowed active-site cleft, in the substrate-binding direction. The, mini-chain fills the ... [(full description)]

About this Structure

8PCH is a [Single protein] structure of sequence from [Sus scrofa]. Active as [Hydrolase], with EC number [3.4.22.16]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].

Reference

Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function., Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D, Structure. 1998 Jan 15;6(1):51-61. PMID:9493267

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