1w24: Difference between revisions

Revision as of 15:54, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1w24.png

Template:STRUCTURE 1w24

CRYSTAL STRUCTURE OF HUMAN VPS29CRYSTAL STRUCTURE OF HUMAN VPS29

Template:ABSTRACT PUBMED 15788412

About this StructureAbout this Structure

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

ReferenceReference

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

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OCA

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-'''CRYSTAL STRUCTURE OF HUMAN VPS29'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15788412}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15788412 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15788412}}
 ==About this Structure==
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 [[Category: Alpha-beta-beta-alpha sandwich]]
 [[Category: Vacuolar protein sorting protein]]
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