1a64: Difference between revisions

Revision as of 09:52, 2 May 2008

ENGINEERING A MISFOLDED FORM OF RAT CD2

OverviewOverview

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.

About this StructureAbout this Structure

1A64 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 Fri May 2 09:52:07 2008

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OCA

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 [[Image:1a64.gif|left|200px]]
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 '''ENGINEERING A MISFOLDED FORM OF RAT CD2'''
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 [[Category: Head, J G.]]
 [[Category: Murray, A J.]]
-[[Category: domain swapping]]
+[[Category: Domain swapping]]
-[[Category: hinge loop]]
+[[Category: Hinge loop]]
-[[Category: oligomer evolution]]
+[[Category: Oligomer evolution]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:52:07 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:04 2008''