We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qye

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1qye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qye, resolution 2.10&Aring;" /> '''Crystal Structure of...)
Current revision (05:57, 23 August 2023) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1qye.gif|left|200px]]<br /><applet load="1qye" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1qye, resolution 2.10&Aring;" />
 
-
'''Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine'''<br />
 
-
==Overview==
+
==Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine==
-
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.
+
<StructureSection load='1qye' size='340' side='right'caption='[[1qye]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1qye]] is a 1 chain structure with sequence from [https://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=1QYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QYE FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CDY:2-CHLORODIDEOXYADENOSINE'>CDY</scene>, <scene name='pdbligand=M2M:1-METHOXY-2-(2-METHOXYETHOXY)ETHANE'>M2M</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qye OCA], [https://pdbe.org/1qye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qye RCSB], [https://www.ebi.ac.uk/pdbsum/1qye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qye ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ENPL_CANLF ENPL_CANLF] Molecular chaperone that functions in the processing and transport of secreted proteins. When associated with CNPY3, required for proper folding of Toll-like receptors. Functions in endoplasmic reticulum associated degradation (ERAD). Has ATPase activity (By similarity).
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qy/1qye_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1qye ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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==
+
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<ref>PMID:12970348</ref>
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QYE OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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]
+
</div>
-
[[Category: Canis lupus familiaris]]
+
<div class="pdbe-citations 1qye" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Gewirth, D.T.]]
+
-
[[Category: Jivan, A.]]
+
-
[[Category: Nicchitta, C.V.]]
+
-
[[Category: Soldano, K.L.]]
+
-
[[Category: CDY]]
+
-
[[Category: M2M]]
+
-
[[Category: 2-chlorodideoxyadenosine]]
+
-
[[Category: 2cldda]]
+
-
[[Category: gp96]]
+
-
[[Category: grp94]]
+
-
[[Category: hsp90]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:07:29 2007''
+
==See Also==
 +
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Canis lupus familiaris]]
 +
[[Category: Large Structures]]
 +
[[Category: Gewirth DT]]
 +
[[Category: Jivan A]]
 +
[[Category: Nicchitta CV]]
 +
[[Category: Soldano KL]]

Current revision

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine

PDB ID 1qye

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qye"
Personal tools