1dkd: Difference between revisions

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[[Image:1dkd.gif|left|200px]]
[[Image:1dkd.gif|left|200px]]


{{Structure
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|RELATEDENTRY=[[1dk7|1DK7]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dkd OCA], [http://www.ebi.ac.uk/pdbsum/1dkd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dkd RCSB]</span>
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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'''
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[[Category: Chen, L.]]
[[Category: Chen, L.]]
[[Category: Sigler, P B.]]
[[Category: Sigler, P B.]]
[[Category: hsp60]]
[[Category: Hsp60]]
[[Category: molecular chaperon]]
[[Category: Molecular chaperon]]
[[Category: peptide binding groove formed by paired helices substrate peptide in beta-sheet]]
[[Category: Peptide binding groove formed by paired helices substrate peptide in beta-sheet]]
[[Category: peptide selection]]
[[Category: Peptide selection]]
[[Category: phage display]]
[[Category: Phage display]]
[[Category: protein folding]]
[[Category: Protein folding]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:43:13 2008''

Revision as of 13:57, 2 May 2008

File:1dkd.gif

Template:STRUCTURE 1dkd

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


OverviewOverview

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.

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 Page seeded by OCA on Fri May 2 13:57:00 2008

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