1qg3

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1qg3, resolution 2.15Å

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CRYSTAL STRUCTURE OF A TANDEM PAIR OF FIBRONECTIN TYPE III DOMAINS FROM THE CYTOPLASMIC TAIL OF INTEGRIN ALPHA6 BETA4

Contents

Overview

The integrin alpha6beta4 is an essential component of hemidesmosomes but, it also plays a dynamic role in invasive carcinoma cells. The cytoplasmic, tail of the beta4 subunit is uniquely large among integrins and includes, two pairs of fibronectin type III domains separated by a connecting, segment. Here we describe the crystal structure of the first tandem domain, pair, a module that is critical for alpha6beta4 function. The structure, reveals a novel interdomain interface and candidate protein-binding sites, including a large acidic cleft formed from the surfaces of both domains, and a prominent loop that is reminiscent of the RGD integrin-binding loop, of fibronectin. This is the first crystal structure of either a, hemidesmosome component or an integrin cytoplasmic domain, and it will, enable the intracellular functions of alpha6beta4 to be dissected at the, atomic level.

Disease

Known diseases associated with this structure: Epidermolysis bullosa of hands and feet OMIM:[147557], Epidermolysis bullosa, generalized atrophic benign OMIM:[147557], Epidermolysis bullosa, junctional, with pyloric atresia OMIM:[147557]

About this Structure

1QG3 is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a tandem pair of fibronectin type III domains from the cytoplasmic tail of integrin alpha6beta4., de Pereda JM, Wiche G, Liddington RC, EMBO J. 1999 Aug 2;18(15):4087-95. PMID:10428948

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