1r4a
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(New page: 200px<br /> <applet load="1r4a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4a, resolution 2.3Å" /> '''Crystal Structure of...)
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Revision as of 16:53, 12 November 2007
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Crystal Structure of GTP-bound ADP-ribosylation Factor Like Protein 1 (Arl1) and GRIP Domain of Golgin245 COMPLEX
Overview
Recruitment of the GRIP domain golgins to the trans-Golgi network is, mediated by Arl1, a member of the ARF/Arl small GTPase family, through, interaction between their GRIP domains and Arl1-GTP. The crystal structure, of Arl1-GTP in complex with the GRIP domain of golgin-245 shows that, Arl1-GTP interacts with the GRIP domain predominantly in a hydrophobic, manner, with the switch II region conferring the main recognition surface., The involvement of the switch and interswitch regions in the interaction, between Arl1-GTP and GRIP accounts for the specificity of GRIP domain for, Arl1-GTP. Mutations that abolished the Arl1-mediated Golgi localization of, GRIP domain golgins have been mapped on the interface between Arl1-GTP and, GRIP. Notably, the GRIP domain forms a homodimer in which each subunit, interacts separately with one Arl1-GTP. Mutations disrupting the GRIP, domain dimerization also abrogated its Golgi targeting, suggesting that, the dimeric form of GRIP domain is a functional unit.
About this Structure
1R4A is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with MG and GNP as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1., Wu M, Lu L, Hong W, Song H, Nat Struct Mol Biol. 2004 Jan;11(1):86-94. Epub 2003 Dec 29. PMID:14718928
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