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1w24
From Proteopedia
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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: | + | [[Category: Vacuolar protein sorting protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:02:51 2008'' | |
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Revision as of 10:02, 3 May 2008
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
