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1upt

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(New page: 200px<br /> <applet load="1upt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1upt, resolution 1.70&Aring;" /> '''STRUCTURE OF A COMP...)
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Revision as of 18:24, 29 October 2007

Image:1upt.gif

1upt, resolution 1.70Å

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STRUCTURE OF A COMPLEX OF THE GOLGIN-245 GRIP DOMAIN WITH ARL1

Overview

Golgins are large coiled-coil proteins that play a role in Golgi structure, and vesicle traffic. The Arf-like GTPase Arl1 regulates the translocation, of GRIP domain-containing golgins to Golgi membranes. We report here the, 1.7 A resolution structure of human Arl1-GTP in a complex with the GRIP, domain of golgin-245. The structure reveals that the GRIP domain consists, of an S-shaped arrangement of three helices. The domain forms a homodimer, that binds two Arl1-GTPs using two helices from each monomer. The, structure is consistent with golgin-245 forming parallel coiled-coils and, suggests how Arl1-GTP/GRIP complexes interact with Golgi membranes via the, N termini of Arl1-GTP and the C-terminal tails of the GRIP domains. In, cells, bivalent association with Arl1-GTP would increase ... [(full description)]

About this Structure

1UPT is a [Protein complex] structure of sequences from [Homo sapiens] with MG and GTP as [ligands]. Full crystallographic information is available from [OCA].

Reference

Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus., Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S, Mol Cell. 2003 Oct;12(4):863-74. PMID:14580338

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