1cmz: Difference between revisions
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[[Image:1cmz.gif|left|200px]] | [[Image:1cmz.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING''' | {{Structure | ||
|PDB= 1cmz |SIZE=350|CAPTION= <scene name='initialview01'>1cmz</scene> | |||
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'''SOLUTION STRUCTURE OF GAIP (GALPHA INTERACTING PROTEIN): A REGULATOR OF G PROTEIN SIGNALING''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1CMZ is a [ | 1CMZ is a [[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== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10452897 10452897] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gaip]] | [[Category: gaip]] | ||
[[Category: regulator of g protein]] | [[Category: regulator of g protein]] | ||
[[Category: | [[Category: rg]] | ||
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Revision as of 11:26, 20 March 2008
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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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