1dkd: Difference between revisions

Revision as of 23:12, 30 June 2008

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File:1dkd.png

Template:STRUCTURE 1dkd

CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEXCRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX

Template:ABSTRACT PUBMED 10619429

About this StructureAbout this Structure

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

ReferenceReference

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity., Chen L, Sigler PB, Cell. 1999 Dec 23;99(7):757-68. PMID:10619429

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-'''CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX'''
+===CRYSTAL STRUCTURE OF A GROEL (APICAL DOMAIN) AND A DODECAMERIC PEPTIDE COMPLEX===
-==Overview==
+<!--
-The chaperonin GroEL is a double toriodal assembly that with its cochaperonin GroES facilitates protein folding with an ATP-dependent mechanism. Nonnative conformations of diverse protein substrates bind to the apical domains surrounding the opening of the double toroid's central cavity. Using phage display, we have selected peptides with high affinity for the isolated apical domain. We have determined the crystal structures of the complexes formed by the most strongly bound peptide with the isolated apical domain, and with GroEL. The peptide interacts with the groove between paired alpha helices in a manner similar to that of the GroES mobile loop. Our structural analysis, combined with other results, suggests that various modes of molecular plasticity are responsible for tight promiscuous binding of nonnative substrates and their release into the shielded cis assembly.
+The line below this paragraph, {{ABSTRACT_PUBMED_10619429}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10619429}}
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 [[Category: Phage display]]
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