1qy8

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[[Image:1qy8.jpg|left|200px]]<br /><applet load="1qy8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qy8.jpg|left|200px]]
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caption="1qy8, resolution 1.85&Aring;" />
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'''Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol'''<br />
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{{Structure
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|PDB= 1qy8 |SIZE=350|CAPTION= <scene name='initialview01'>1qy8</scene>, resolution 1.85&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=RDI:RADICICOL'>RDI</scene>
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|ACTIVITY=
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|GENE= TRA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris])
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}}
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'''Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QY8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] with <scene name='pdbligand=RDI:'>RDI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY8 OCA].
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1QY8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QY8 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12970348 12970348]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12970348 12970348]
[[Category: Canis lupus familiaris]]
[[Category: Canis lupus familiaris]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: radicicol]]
[[Category: radicicol]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:44:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:27 2008''

Revision as of 11:44, 20 March 2008


PDB ID 1qy8

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands:
Gene: TRA1 (Canis lupus familiaris)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with Radicicol


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

1QY8 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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