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| Crystal structure of a G(A) protein beta gamma dimer at 2.1 angstrom resolution |
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| Author(s): Sondek J, Bohm A, Lambright DG, Hamm HE, Sigler PB |
| Source: NATURE Volume: 379 Issue: 6563 Pages: 369-374 Published: JAN 25 1996 |
| Times Cited: 566 References: 32 |
| Abstract: MANY signalling cascades use seven-helical transmembrane receptors coupled to heterotrimeric G proteins (G(alpha beta gamma)) to convert extracellular signals into intracellular responses(1). Upon nucleotide exchange catalysed by activated receptors, heterotrimers dissociate into GTP-bound G(alpha) subunits and G(beta gamma) dimers, either of which can modulate many downstream effectors(2,3). Here we use multiwavelength anomalous diffraction data to solve the crystal structure of the beta gamma dimer of the G protein transducin. The beta-subunit is primarily a seven-bladed beta-propeller that is partially encircled by an extended gamma-subunit. The beta-propeller, which contains seven structurally similar WD repeats, defines the stereochemistry of the WD repeat and the probable architecture of all WD-repeat-containing domains. The structure details interactions between G protein beta- and gamma-subunits and highlights regions implicated in effector modulation for the conserved family of G protein beta gamma dimers. |
| Document Type: Article |
| Language: English |
Addresses:
1. YALE UNIV, DEPT MOLEC BIOPHYS & BIOCHEM, NEW HAVEN, CT 06510 USA
2. YALE UNIV, HOWARD HUGHES MED INST, NEW HAVEN, CT 06510 USA
3. UNIV ILLINOIS, DEPT PHYSIOL & BIOPHYS, CHICAGO, IL 60612 USA |
| Publisher: MACMILLAN MAGAZINES LTD, 4 LITTLE ESSEX STREET, LONDON, ENGLAND WC2R 3LF |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: TR323 |
| ISSN: 0028-0836 |
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