Abstract
p115RhoGEF, a guanine nucleotide exchange factor for Rho GTPase, is also a GTPase activating protein (GAP) for G(12) and G(13) heterotrimeric G alpha subunits. Near its N-terminus, p115RhoGEF contains a domain (rgRGS) with remote sequence identity to RGS (regulators of G protein signaling) domains. The rgRGS domain is necessary but not sufficient for the GAP activity of p115RhoGEF. The 1.9 A resolution crystal structure of the rgRGS domain shows structural similarity to RGS domains but possesses a C-terminal extension that folds into a layer of helices that pack against the hydrophobic core of the domain. Mutagenesis experiments show that rgRGS may form interactions with G alpha(13) that are analogous to those in complexes of RGS proteins with their G alpha substrates.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Crystallography, X-Ray
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Guanine Nucleotide Exchange Factors / chemistry*
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Guanine Nucleotide Exchange Factors / genetics
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Guanine Nucleotide Exchange Factors / metabolism*
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Heterotrimeric GTP-Binding Proteins / chemistry
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Heterotrimeric GTP-Binding Proteins / metabolism
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Humans
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Models, Molecular
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Molecular Sequence Data
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Mutation / genetics
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Peptide Fragments / chemistry
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Peptide Fragments / genetics
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Peptide Fragments / metabolism
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Protein Binding
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Protein Structure, Tertiary
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Protein Subunits
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Rho Guanine Nucleotide Exchange Factors
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Sequence Alignment
Substances
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Guanine Nucleotide Exchange Factors
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Peptide Fragments
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Protein Subunits
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Rho Guanine Nucleotide Exchange Factors
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Heterotrimeric GTP-Binding Proteins