1wms

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|ACTIVITY=
|ACTIVITY=
|GENE= Rab9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= Rab9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wms OCA], [http://www.ebi.ac.uk/pdbsum/1wms PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wms RCSB]</span>
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[[Category: Wang, Y.]]
[[Category: Wang, Y.]]
[[Category: Zhou, X E.]]
[[Category: Zhou, X E.]]
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[[Category: GDP]]
 
[[Category: gtpase]]
[[Category: gtpase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:07:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:38:21 2008''

Revision as of 21:38, 30 March 2008


PDB ID 1wms

Drag the structure with the mouse to rotate
, resolution 1.25Å
Ligands:
Gene: Rab9 (Homo sapiens)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target


Overview

Rab GTPases and their effectors facilitate vesicular transport by tethering donor vesicles to their respective target membranes. Rab9 mediates late endosome to trans-Golgi transport and has recently been found to be a key cellular component for human immunodeficiency virus-1, Ebola, Marburg, and measles virus replication, suggesting that it may be a novel target in the development of broad spectrum antiviral drugs. As part of our structure-based drug design program, we have determined the crystal structure of a C-terminally truncated human Rab9 (residues 1-177) to 1.25-A resolution. The overall structure shows a characteristic nucleotide binding fold consisting of a six-stranded beta-sheet surrounded by five alpha-helices with a tightly bound GDP molecule in the active site. Structure-based sequence alignment of Rab9 with other Rab proteins reveals that its active site consists of residues highly conserved in the Rab GTPase family, implying a common catalytic mechanism. However, Rab9 contains seven regions that are significantly different in conformation from other Rab proteins. Some of those regions coincide with putative effector-binding sites and switch I and switch II regions identified by structure/sequence alignments. The Rab9 structure at near atomic resolution provides an excellent model for structure-based antiviral drug design.

About this Structure

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

Reference

High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target., Chen L, DiGiammarino E, Zhou XE, Wang Y, Toh D, Hodge TW, Meehan EJ, J Biol Chem. 2004 Sep 17;279(38):40204-8. Epub 2004 Jul 19. PMID:15263003

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