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1qye
From Proteopedia
(New page: 200px<br /><applet load="1qye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qye, resolution 2.10Å" /> '''Crystal Structure of...) |
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| - | [[Image:1qye.gif|left|200px]]<br /><applet load="1qye" size=" | + | [[Image:1qye.gif|left|200px]]<br /><applet load="1qye" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qye, resolution 2.10Å" /> | caption="1qye, resolution 2.10Å" /> | ||
'''Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine'''<br /> | '''Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine'''<br /> | ||
==Overview== | ==Overview== | ||
| - | GRP94, the endoplasmic reticulum (ER) paralog of the chaperone Hsp90, plays an essential role in the structural maturation or secretion of a | + | 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== | ==About this Structure== | ||
| - | 1QYE 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 CDY and M2M as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1QYE 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=CDY:'>CDY</scene> and <scene name='pdbligand=M2M:'>M2M</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QYE OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gewirth, D | + | [[Category: Gewirth, D T.]] |
[[Category: Jivan, A.]] | [[Category: Jivan, A.]] | ||
| - | [[Category: Nicchitta, C | + | [[Category: Nicchitta, C V.]] |
| - | [[Category: Soldano, K | + | [[Category: Soldano, K L.]] |
[[Category: CDY]] | [[Category: CDY]] | ||
[[Category: M2M]] | [[Category: M2M]] | ||
| Line 25: | Line 25: | ||
[[Category: hsp90]] | [[Category: hsp90]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:04 2008'' |
Revision as of 12:45, 21 February 2008
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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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 14:45:04 2008
Categories: Canis lupus familiaris | Single protein | Gewirth, D T. | Jivan, A. | Nicchitta, C V. | Soldano, K L. | CDY | M2M | 2-chlorodideoxyadenosine | 2cldda | Gp96 | Grp94 | Hsp90
