1a7b: Difference between revisions

Revision as of 16:17, 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:1a7b.png

Template:STRUCTURE 1a7b

ENGINEERING A MISFOLDED FORM OF CD2ENGINEERING A MISFOLDED FORM OF CD2

Template:ABSTRACT PUBMED 9731771

About this StructureAbout this Structure

1A7B is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Engineering an intertwined form of CD2 for stability and assembly., Murray AJ, Head JG, Barker JJ, Brady RL, Nat Struct Biol. 1998 Sep;5(9):778-82. PMID:9731771

Page seeded by OCA on Mon Jun 30 16:17:51 2008

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OCA

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-==Overview==
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-The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.
+The line below this paragraph, {{ABSTRACT_PUBMED_9731771}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_9731771}}
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 [[Category: Protein evolution]]
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