1ckr
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(New page: 200px<br /><applet load="1ckr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ckr" /> '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE HE...)
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Revision as of 10:25, 20 November 2007
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HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES
Overview
The three-dimensional structure for the substrate-binding domain of the, mammalian chaperone protein Hsc70 of the 70 kDa heat shock class (HSP70), is presented. This domain includes residues 383-540 (18 kDa) and is, necessary for the binding of the chaperone with substrate proteins and, peptides. The high-resolution NMR solution structure is based on 4150, experimental distance constraints leading to an average root-mean-square, precision of 0.38 A for the backbone atoms and 0.76 A for all atoms in the, beta-sandwich sub-domain. The protein is observed to bind residue Leu539, in its hydrophobic substrate-binding groove by intramolecular interaction., The position of a helical latch differs dramatically from what is observed, in the crystal and solution structures of the homologous prokaryotic, chaperone DnaK. In the Hsc70 structure, the helix lies in a hydrophobic, groove and is anchored by a buried salt-bridge. Residues involved in this, salt-bridge appear to be important for the allosteric functioning of the, protein. A mechanism for interdomain allosteric modulation of, substrate-binding is proposed. It involves large-scale movements of the, helical domain, redefining the location of the hinge area that enables, such motions.
About this Structure
1CKR is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70., Morshauser RC, Hu W, Wang H, Pang Y, Flynn GC, Zuiderweg ER, J Mol Biol. 1999 Jun 25;289(5):1387-403. PMID:10373374
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