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| {{STRUCTURE_1u2o| PDB=1u2o | SCENE= }} | | {{STRUCTURE_1u2o| PDB=1u2o | SCENE= }} |
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| '''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=== |
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| ==Overview==
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| 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. |
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| | {{ABSTRACT_PUBMED_12970348}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[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'' |