1QG3

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

Summary for 1QG3

• Entry DOI: 10.2210/pdb1qg3/pdb
• Descriptor: PROTEIN (INTEGRIN BETA-4 SUBUNIT), CACODYLATE ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: integrin, hemidesmosome, fibronectin, carcinoma, structural protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 43898.84

Authors

de Pereda, J.M.,Wiche, G.,Liddington, R.C. (deposition date: 1999-04-19, release date: 1999-08-20, Last modification date: 2023-12-27)

Primary citation

de Pereda, J.M.,Wiche, G.,Liddington, R.C.
Crystal structure of a tandem pair of fibronectin type III domains from the cytoplasmic tail of integrin alpha6beta4.
EMBO J., 18:4087-4095, 1999

PubMed 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.

PubMed: 10428948
DOI: 10.1093/emboj/18.15.4087

Experimental method

X-RAY DIFFRACTION (2.15 Å)