Literature DB >> 8208289

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein.

D G Lambright1, J P Noel, H E Hamm, P B Sigler.   

Abstract

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.

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Year:  1994        PMID: 8208289     DOI: 10.1038/369621a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  127 in total

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Review 4.  Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins.

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8.  Differences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins.

Authors:  Janice C Jones; Alan M Jones; Brenda R S Temple; Henrik G Dohlman
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Review 9.  Implications of non-canonical G-protein signaling for the immune system.

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Journal:  Cell Signal       Date:  2014-02-28       Impact factor: 4.315

Review 10.  G-protein signaling: back to the future.

Authors:  C R McCudden; M D Hains; R J Kimple; D P Siderovski; F S Willard
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