1a7b

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Image:1a7b.gif

1a7b, resolution 3.1Å

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ENGINEERING A MISFOLDED FORM OF CD2

Overview

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 Structure

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

Reference

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

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