1tag

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Image:1tag.gif

1tag, resolution 1.8Å

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STRUCTURAL DETERMINANTS FOR ACTIVATION OF THE ALPHA-SUBUNIT OF A HETEROTRIMERIC G PROTEIN

Overview

The 1.8 A crystal structure of transducin alpha.GDP, when compared to that, of the activated complex with GTP-gamma S, reveals the nature of the, conformational changes that occur on activation of a heterotrimeric, G-protein alpha-subunit. Structural changes initiated by direct contacts, with the terminal phosphate of GTP propagate to regions that have been, implicated in effector activation. The changes are distinct from those, observed in other members of the GTPase superfamily.

About this Structure

1TAG is a Single protein structure of sequence from Bos taurus with MG and GDP as ligands. Full crystallographic information is available from OCA.

Reference

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein., Lambright DG, Noel JP, Hamm HE, Sigler PB, Nature. 1994 Jun 23;369(6482):621-8. PMID:8208289

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