1ckr
From Proteopedia
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| - | [[Image:1ckr.gif|left|200px]] | + | [[Image:1ckr.gif|left|200px]] |
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| - | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES''' | + | {{Structure |
| + | |PDB= 1ckr |SIZE=350|CAPTION= <scene name='initialview01'>1ckr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CKR is a [ | + | 1CKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10373374 10373374] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:25:38 2008'' |
Revision as of 08:25, 20 March 2008
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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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