This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1u2o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u2o.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1u2o.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u2o| PDB=1u2o | SCENE= }}
{{STRUCTURE_1u2o| PDB=1u2o | SCENE= }}
-
'''Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca'''
+
===Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12970348}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12970348 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12970348}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Hsp90]]
[[Category: Hsp90]]
[[Category: Neca]]
[[Category: Neca]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:40:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:35:31 2008''

Revision as of 11:35, 27 July 2008

Image:1u2o.png

Template:STRUCTURE 1u2o

Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca

Template:ABSTRACT PUBMED 12970348

About this Structure

1U2O is a Single protein structure of sequence from Canis lupus familiaris. This structure supersedes the now removed PDB entry 1qyh. 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 Sun Jul 27 14:35:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u2o"
Personal tools