<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1r4a ConSurf].
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Revision as of 21:05, 9 February 2016
Crystal Structure of GTP-bound ADP-ribosylation Factor Like Protein 1 (Arl1) and GRIP Domain of Golgin245 COMPLEX
1r4a is a 8 chain structure with sequence from Buffalo rat and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[ARL1_RAT] GTP-binding protein. Can activate phospholipase D with very low efficiency (By similarity). Important for normal function of the Golgi apparatus.[1][2] [GOGA4_HUMAN] May play a role in delivery of transport vesicles containing GPI-linked proteins from the trans-Golgi network through its interaction with MACF1.[3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑Lu L, Horstmann H, Ng C, Hong W. Regulation of Golgi structure and function by ARF-like protein 1 (Arl1). J Cell Sci. 2001 Dec;114(Pt 24):4543-55. PMID:11792819
↑Lu L, Hong W. Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell. 2003 Sep;14(9):3767-81. Epub 2003 May 18. PMID:12972563 doi:https://dx.doi.org/10.1091/mbc.E03-01-0864
↑Kakinuma T, Ichikawa H, Tsukada Y, Nakamura T, Toh BH. Interaction between p230 and MACF1 is associated with transport of a glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell periphery. Exp Cell Res. 2004 Aug 15;298(2):388-98. PMID:15265687 doi:https://dx.doi.org/10.1016/j.yexcr.2004.04.047
↑Wu M, Lu L, Hong W, Song H. Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1. Nat Struct Mol Biol. 2004 Jan;11(1):86-94. Epub 2003 Dec 29. PMID:14718928 doi:10.1038/nsmb714
