1QYE
Crystal Structure of the N-domain of the ER Hsp90 chaperone GRP94 in complex with 2-chlorodideoxyadenosine
Summary for 1QYE
| Entry DOI | 10.2210/pdb1qye/pdb |
| Related | 1QY5 1QY8 |
| Descriptor | Endoplasmin, 2-CHLORODIDEOXYADENOSINE, 1-METHOXY-2-(2-METHOXYETHOXY)ETHANE, ... (4 entities in total) |
| Functional Keywords | grp94, gp96, hsp90, 2cldda, 2-chlorodideoxyadenosine, chaperone |
| Biological source | Canis lupus familiaris (dog) |
| Cellular location | Endoplasmic reticulum lumen: P41148 |
| Total number of polymer chains | 1 |
| Total formula weight | 31046.18 |
| Authors | Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T. (deposition date: 2003-09-10, release date: 2003-11-11, Last modification date: 2023-08-23) |
| Primary citation | Soldano, K.L.,Jivan, A.,Nicchitta, C.V.,Gewirth, D.T. Structure of the N-terminal Domain of GRP94. Basis for Ligand Specificity and Regulation J.Biol.Chem., 278:48330-48338, 2003 Cited by PubMed 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. PubMed: 12970348DOI: 10.1074/jbc.M308661200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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