1cci: Difference between revisions

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[[Image:1cci.gif|left|200px]]
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[[Image:1cci.png|left|200px]]


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{{STRUCTURE_1cci|  PDB=1cci  |  SCENE=  }}  
{{STRUCTURE_1cci|  PDB=1cci  |  SCENE=  }}  


'''HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP'''
===HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP===




==Overview==
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Conformational changes that gate the access of substrates or ligands to an active site are important features of enzyme function. In this report, we describe an unusual example of a structural rearrangement near a buried artificial cavity in cytochrome c peroxidase that occurs on binding protonated benzimidazole. A hinged main-chain rotation at two residues (Pro 190 and Asn 195) results in a surface loop rearrangement that opens a large solvent-accessible channel for the entry of ligands to an otherwise inaccessible binding site. The trapping of this alternate conformational state provides a unique view of the extent to which protein dynamics can allow small molecule penetration into buried protein cavities.
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{{ABSTRACT_PUBMED_8673607}}


==About this Structure==
==About this Structure==
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[[Category: Polymorphism]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
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Revision as of 17:33, 30 June 2008

File:1cci.png

Template:STRUCTURE 1cci

HOW FLEXIBLE ARE PROTEINS? TRAPPING OF A FLEXIBLE LOOP

Template:ABSTRACT PUBMED 8673607

About this Structure

1CCI is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A ligand-gated, hinged loop rearrangement opens a channel to a buried artificial protein cavity., Fitzgerald MM, Musah RA, McRee DE, Goodin DB, Nat Struct Biol. 1996 Jul;3(7):626-31. PMID:8673607

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