1ckr: Difference between revisions

Revision as of 20:53, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ckr.png

Template:STRUCTURE 1ckr

HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUESHIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES

Template:ABSTRACT PUBMED 10373374

About this StructureAbout this Structure

1CKR is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

ReferenceReference

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ckr.gif|left|200px]]
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 {{STRUCTURE_1ckr|  PDB=1ckr  |  SCENE=  }}
-'''HIGH RESOLUTION SOLUTION STRUCTURE OF THE HEAT SHOCK COGNATE-70 KD SUBSTRATE BINDING DOMAIN OBTAINED BY MULTIDIMENSIONAL NMR TECHNIQUES'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10373374}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10373374 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10373374}}
 ==About this Structure==
-CKR 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].
+CKR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CKR OCA].
 ==Reference==
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 [[Category: Peptide binding]]
 [[Category: Protein folding]]
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