1qmb

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spinqualitylabelsall models 1qmb, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CLEAVED ALPHA-1-ANTITRYPSIN POLYMER

Overview

The function of the serpins as proteinase inhibitors depends on their, ability to insert the cleaved reactive centre loop as the fourth strand in, the main A beta-sheet of the molecule upon proteolytic attack at the, reactive centre, P1-P1'. This mechanism is vulnerable to mutations which, result in inappropriate intra- or intermolecular loop insertion in the, absence of cleavage. Intermolecular loop insertion is known as serpin, polymerisation and results in a variety of diseases, most notably liver, cirrhosis resulting from mutations of the prototypical serpin, alpha1-antitrypsin. We present here the 2.6 A structure of a polymer of, alpha1-antitrypsin cleaved six residues N-terminal to the reactive centre, P7-P6 (Phe352-Leu353). After self insertion of P14 to P7, intermolecular, linkage ... [(full description)]

About this Structure

1QMB is a [Protein complex] structure of sequences from [Homo sapiens]. Full crystallographic information is available from [OCA].

Reference

A 2.6 A structure of a serpin polymer and implications for conformational disease., Huntington JA, Pannu NS, Hazes B, Read RJ, Lomas DA, Carrell RW, J Mol Biol. 1999 Oct 29;293(3):449-55. PMID:10543942

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