1qg3

From Proteopedia

Revision as of 12:39, 21 February 2008

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

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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