1w24

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[[Image:1w24.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w24 OCA], [http://www.ebi.ac.uk/pdbsum/1w24 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w24 RCSB]</span>
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'''CRYSTAL STRUCTURE OF HUMAN VPS29'''
'''CRYSTAL STRUCTURE OF HUMAN VPS29'''
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[[Category: Teng, M.]]
[[Category: Teng, M.]]
[[Category: Wang, D.]]
[[Category: Wang, D.]]
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[[Category: alpha-beta-beta-alpha sandwich]]
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[[Category: Alpha-beta-beta-alpha sandwich]]
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[[Category: vacuolar protein sorting protein]]
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[[Category: Vacuolar protein sorting protein]]
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Revision as of 10:02, 3 May 2008

Template:STRUCTURE 1w24

CRYSTAL STRUCTURE OF HUMAN VPS29


Overview

Vacuolar protein sorting protein 29 (Vps29p), which is involved in retrograde trafficking from prevacuolar endosomes to the trans-Golgi network, performs its biological functions by participating in the formation of a "retromer complex." In human cells, this complex comprises four conserved proteins: hVps35p, hVps29p, hVps26p, and sorting nexin 1 protein (SNX1). Here, we report the crystal structure of hVps29p at 2.1 Angstroms resolution, the first three-dimensional structure of the retromer subunits. This novel structure adopts a four-layered alpha-beta-beta-alpha sandwich fold. hVps29p contains a metal-binding site that is very similar to the active sites of some proteins of the phosphodiesterase/nuclease protein family, indicating that hVps29p may carry out chemically similar functions. Structure and sequence conservation analysis suggests that hVps29p contains two protein-protein interaction sites. One site, which potentially serves as the interface between hVps29p and hVps35p, comprises 5 conserved hydrophobic and 8 hydrophilic residues. The other site is relatively more hydrophilic and may serve as a binding interface with hVps26p, SNX1, or other target proteins.

About this Structure

1W24 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites., Wang D, Guo M, Liang Z, Fan J, Zhu Z, Zang J, Zhu Z, Li X, Teng M, Niu L, Dong Y, Liu P, J Biol Chem. 2005 Jun 17;280(24):22962-7. Epub 2005 Mar 23. PMID:15788412 Page seeded by OCA on Sat May 3 13:02:51 2008

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