1QY5: Crystal Structure Of The N-Domain Of The Er Hsp90 Chaperone Grp94 In Complex With The Specific Ligand Neca

Citation:
Abstract
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.
PDB ID: 1QY5Download
MMDB ID: 25424
PDB Deposition Date: 2003/9/9
Updated in MMDB: 2003/12
Experimental Method:
x-ray diffraction
Resolution: 1.75  Å
Source Organism:

*This structure record is obsolete.

Molecular Components in 1QY5
Label Count Molecule
Protein (1 molecule)
1
Endoplasmin
Molecule annotation
Chemicals (2 molecules)
1
1
2
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.