1u2o
Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca
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| , resolution 2.10Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | TRA1 (Canis lupus familiaris) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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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