G proteins, effecters and GAPs: Structure and mechanism

Stephen R. Sprang

doi:10.1016/S0959-440X(97)80157-1

G proteins, effecters and GAPs: Structure and mechanism

Stephen R. Sprang

Division of Biological and Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

130 Scopus citations

Abstract

G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

Original language	English
Pages (from-to)	849-856
Number of pages	8
Journal	Current Opinion in Structural Biology
Volume	7
Issue number	6
DOIs	https://doi.org/10.1016/S0959-440X(97)80157-1
State	Published - Dec 1997

Funding

1 thank Mark Wall for assistance in the production of figures. Research has been supported in part by grants from the National Institutes of Health

Funder number
R01DK046371

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10.1016/S0959-440X(97)80157-1

Cite this

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title = "G proteins, effecters and GAPs: Structure and mechanism",

abstract = "G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.",

author = "Sprang, \{Stephen R.\}",

note = "Funding Information: 1 thank Mark Wall for assistance in the production of figures. Research has been supported in part by grants from the National Institutes of Health",

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PY - 1997/12

Y1 - 1997/12

N2 - G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

AB - G proteins form a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effecters. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

UR - https://www.scopus.com/pages/publications/0031283407

U2 - 10.1016/S0959-440X(97)80157-1

DO - 10.1016/S0959-440X(97)80157-1

M3 - Article

C2 - 9434906

AN - SCOPUS:0031283407

SN - 0959-440X

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EP - 856

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 6

ER -

G proteins, effecters and GAPs: Structure and mechanism

Abstract

Funding

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