1qye
From Proteopedia
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|PDB= 1qye |SIZE=350|CAPTION= <scene name='initialview01'>1qye</scene>, resolution 2.10Å | |PDB= 1qye |SIZE=350|CAPTION= <scene name='initialview01'>1qye</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CDY:2-CHLORODIDEOXYADENOSINE'>CDY</scene> | + | |LIGAND= <scene name='pdbligand=CDY:2-CHLORODIDEOXYADENOSINE'>CDY</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | |GENE= TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qy5|1QY5]], [[1qy8|1QY8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qye OCA], [http://www.ebi.ac.uk/pdbsum/1qye PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qye RCSB]</span> | ||
}} | }} | ||
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[[Category: Nicchitta, C V.]] | [[Category: Nicchitta, C V.]] | ||
[[Category: Soldano, K L.]] | [[Category: Soldano, K L.]] | ||
| - | [[Category: CDY]] | ||
| - | [[Category: M2M]] | ||
[[Category: 2-chlorodideoxyadenosine]] | [[Category: 2-chlorodideoxyadenosine]] | ||
[[Category: 2cldda]] | [[Category: 2cldda]] | ||
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[[Category: hsp90]] | [[Category: hsp90]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:43 2008'' |
Revision as of 20:20, 30 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | TRA1 (Canis lupus familiaris) | ||||||
| Related: | 1QY5, 1QY8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine
Overview
GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a subset of proteins destined for transport to the cell surface, such as the Toll-like receptors 2 and 4, and IgG, respectively. GRP94 differs from cytoplasmic Hsp90 by exhibiting very weak ATP binding and hydrolysis activity. GRP94 also binds selectively to a series of substituted adenosine analogs. The high resolution crystal structures at 1.75-2.1 A of the N-terminal and adjacent charged domains of GRP94 in complex with N-ethylcarboxamidoadenosine, radicicol, and 2-chlorodideoxyadenosine reveals a structural mechanism for ligand discrimination among hsp90 family members. The structures also identify a putative subdomain that may act as a ligand-responsive switch. The residues of the charged region fold into a disordered loop whose termini are ordered and continue the twisted beta sheet that forms the structural core of the N-domain. This continuation of the beta sheet past the charged domain suggests a structural basis for the association of the N-terminal and middle domains of the full-length chaperone.
About this Structure
1QYE is a Single protein structure of sequence from Canis lupus familiaris. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation., Soldano KL, Jivan A, Nicchitta CV, Gewirth DT, J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11. PMID:12970348
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