1bpr: Difference between revisions

Revision as of 19:30, 30 June 2008

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File:1bpr.png

Template:STRUCTURE 1bpr

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURENMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE

Template:ABSTRACT PUBMED 9609686

About this StructureAbout this Structure

1BPR is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

ReferenceReference

NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction., Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER, Biochemistry. 1998 Jun 2;37(22):7929-40. PMID:9609686

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OCA

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-'''NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE'''
+===NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK, MINIMIZED AVERAGE STRUCTURE===
-==Overview==
+<!--
-The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision of 1.00 A (backbone of the beta-domain) from 1075 experimental restraints obtained from multinuclear, multidimensional NMR experiments. The domain is observed to bind to its own C-terminus and offers a preview of the interaction of this chaperone with other proteins. The bound protein region is tightly held at a single amino acid position (a leucyl residue) that is buried in a deep pocket lined with conserved hydrophobic residues. A second hydrophobic binding site was identified using paramagnetically labeled peptides. It is located in a region close to the N-terminus of the domain and may constitute the allosteric region that links substrate-binding affinity with nucleotide binding in the Hsp70 chaperones.
+The line below this paragraph, {{ABSTRACT_PUBMED_9609686}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9609686 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9609686}}
 ==About this Structure==
-BPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPR OCA].
+BPR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BPR OCA].
 ==Reference==
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 [[Category: Peptide binding]]
 [[Category: Protein folding]]
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