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. 1999 Aug 2;18(15):4087-95.
doi: 10.1093/emboj/18.15.4087.

Crystal Structure of a Tandem Pair of Fibronectin Type III Domains From the Cytoplasmic Tail of Integrin alpha6beta4

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Free PMC article

Crystal Structure of a Tandem Pair of Fibronectin Type III Domains From the Cytoplasmic Tail of Integrin alpha6beta4

J M de Pereda et al. EMBO J. .
Free PMC article

Abstract

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.

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