1agr: Difference between revisions
New page: left|200px<br /><applet load="1agr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1agr, resolution 2.8Å" /> '''COMPLEX OF ALF4-ACTIV... |
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[[Image:1agr.gif|left|200px]]<br /><applet load="1agr" size=" | [[Image:1agr.gif|left|200px]]<br /><applet load="1agr" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1agr, resolution 2.8Å" /> | caption="1agr, resolution 2.8Å" /> | ||
'''COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4'''<br /> | '''COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4'''<br /> | ||
==Overview== | ==Overview== | ||
RGS proteins are GTPase activators for heterotrimeric G proteins. We | RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors. | ||
==About this Structure== | ==About this Structure== | ||
1AGR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, ALF, GDP and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1AGR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ALF:'>ALF</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AGR OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Sprang, S | [[Category: Sprang, S R.]] | ||
[[Category: Tesmer, J | [[Category: Tesmer, J J.G.]] | ||
[[Category: ALF]] | [[Category: ALF]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:23 2008'' | ||
Revision as of 12:44, 21 February 2008
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COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4
OverviewOverview
RGS proteins are GTPase activators for heterotrimeric G proteins. We report here the 2.8 A resolution crystal structure of the RGS protein RGS4 complexed with G(i alpha1)-Mg2+-GDP-AlF4 . Only the core domain of RGS4 is visible in the crystal. The core domain binds to the three switch regions of G(i alpha1), but does not contribute catalytic residues that directly interact with either GDP or AlF4-. Therefore, RGS4 appears to catalyze rapid hydrolysis of GTP primarily by stabilizing the switch regions of G(i alpha1), although the conserved Asn-128 from RGS4 could also play a catalytic role by interacting with the hydrolytic water molecule or the side chain of Gln-204. The binding site for RGS4 on G(i alpha1) is also consistent with the activity of RGS proteins as antagonists of G(alpha) effectors.
About this StructureAbout this Structure
1AGR is a Protein complex structure of sequences from Rattus norvegicus with , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis., Tesmer JJ, Berman DM, Gilman AG, Sprang SR, Cell. 1997 Apr 18;89(2):251-61. PMID:9108480
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