1cjl

From Proteopedia

Revision as of 18:56, 29 October 2007 by OCA (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search

1cjl, resolution 2.2Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF A CYSTEINE PROTEASE PROFORM

Overview

Cathepsin L is a member of the papain superfamily of cysteine proteases, and, like many other proteases, it is synthesized as an inactive, proenzyme. Its prosegment shows little homology to that of procathepsin B, whose structure, the first for a cysteine protease proenzyme, has been, determined recently. We report here the 3-D structure of a mutant of human, procathepsin L determined at 2.2 A resolution, describe the mode of, binding employed by the prosegment and discuss the molecular basis for, other possible roles of the prosegment. The N-terminal part of the, prosegment is globular and contains three alpha-helices with a small, hydrophobic core built around aromatic side chains. This domain packs, against a loop on the enzyme's surface, with the aromatic side chain from, the ... [(full description)]

About this Structure

1CJL is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.4.22.15]. Full crystallographic information is available from [OCA].

Reference

Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment., Coulombe R, Grochulski P, Sivaraman J, Menard R, Mort JS, Cygler M, EMBO J. 1996 Oct 15;15(20):5492-503. PMID:8896443

Page seeded by OCA on Mon Oct 29 21:01:20 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools