6d28

Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with the specific ligand NECA

spinqualitylabelsall models 6d28, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6d28 is a 1 chain structure. This structure supersedes the now removed PDB entry 1qy5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: M2M, NEC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [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). 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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