1cmz: Difference between revisions

Revision as of 13:07, 21 February 2008

SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING

OverviewOverview

The solution structure of the human protein GAIP (Galpha interacting protein), a regulator of G protein signaling, has been determined by NMR techniques. Dipolar couplings of the oriented protein in two different liquid crystal media have been used in the structure calculation. The solution structure of GAIP is compared to the crystal structure of an homologous protein from rat (RGS4) complexed to the alpha-subunit of a G protein. Some of RGS4 residues involved in the Galpha-RGS binding interface have similar orientations in GAIP (free form), indicating that upon binding these residues do not suffer conformational rearrangements, and therefore, their role does not seem to be restricted to Galpha interaction but also to RGS folding and stability. We suggest that other structural differences between the two proteins may be related to the process of binding as well as to a distinct efficiency in their respective GTPase activating function.

About this StructureAbout this Structure

1CMZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling., de Alba E, De Vries L, Farquhar MG, Tjandra N, J Mol Biol. 1999 Aug 27;291(4):927-39. PMID:10452897

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 '''SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING'''<br />
 ==Overview==
-The solution structure of the human protein GAIP (Galpha interacting, protein), a regulator of G protein signaling, has been determined by NMR, techniques. Dipolar couplings of the oriented protein in two different, liquid crystal media have been used in the structure calculation. The, solution structure of GAIP is compared to the crystal structure of an, homologous protein from rat (RGS4) complexed to the alpha-subunit of a G, protein. Some of RGS4 residues involved in the Galpha-RGS binding, interface have similar orientations in GAIP (free form), indicating that, upon binding these residues do not suffer conformational rearrangements, and therefore, their role does not seem to be restricted to Galpha, interaction but also to RGS folding and stability. We suggest that other, structural differences between the two proteins may be related to the, process of binding as well as to a distinct efficiency in their respective, GTPase activating function.
+The solution structure of the human protein GAIP (Galpha interacting protein), a regulator of G protein signaling, has been determined by NMR techniques. Dipolar couplings of the oriented protein in two different liquid crystal media have been used in the structure calculation. The solution structure of GAIP is compared to the crystal structure of an homologous protein from rat (RGS4) complexed to the alpha-subunit of a G protein. Some of RGS4 residues involved in the Galpha-RGS binding interface have similar orientations in GAIP (free form), indicating that upon binding these residues do not suffer conformational rearrangements, and therefore, their role does not seem to be restricted to Galpha interaction but also to RGS folding and stability. We suggest that other structural differences between the two proteins may be related to the process of binding as well as to a distinct efficiency in their respective GTPase activating function.
 ==About this Structure==
-CMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CMZ OCA].
+CMZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMZ OCA].
 ==Reference==
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 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Alba, E.De.]]
+[[Category: Alba, E De.]]
-[[Category: Farquhar, M.G.]]
+[[Category: Farquhar, M G.]]
 [[Category: Tjandra, N.]]
-[[Category: Vries, L.De.]]
+[[Category: Vries, L De.]]
 [[Category: gaip]]
 [[Category: regulator of g protein]]
 [[Category: rgs]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:23:32 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:07:40 2008''