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1m23

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m23 OCA], [http://www.ebi.ac.uk/pdbsum/1m23 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m23 RCSB]</span>
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[[Category: vesicular transport]]
[[Category: vesicular transport]]
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Revision as of 19:10, 30 March 2008

Image:1m23.gif


PDB ID 1m23

Drag the structure with the mouse to rotate
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF THE DIMERIZED CYTOPLASMIC DOMAIN OF P23 IN SOLUTION


Overview

Coatomer, the coat protein complex of COPI vesicles, is involved in the budding of these vesicles, but the underlying mechanism is unknown. Toward a better understanding of this process, the interaction between coatomer and the cytoplasmic domain of a major transmembrane protein of COPI vesicles, p23, was studied. Interaction of coatomer with this peptide domain results in a conformational change and polymerization of the complex in vitro. This changed conformation also is observed in vivo, i.e., on the surface of authentic, isolated COPI vesicles. An average of four peptides was found associated with one coatomer complex after polymerization. Based on these results, we propose a mechanism by which the induced conformational change of coatomer results in its polymerization, and thus drives formation of the bud on the Golgi membrane during biogenesis of a COPI vesicle.

About this Structure

1M23 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Receptor-induced polymerization of coatomer., Reinhard C, Harter C, Bremser M, Brugger B, Sohn K, Helms JB, Wieland F, Proc Natl Acad Sci U S A. 1999 Feb 16;96(4):1224-8. PMID:9990005

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