Format

Send to

Choose Destination
See comment in PubMed Commons below
Nat Struct Biol. 1998 Sep;5(9):778-82.

Engineering an intertwined form of CD2 for stability and assembly.

Author information

1
Department of Biochemistry and Centre for Molecular Recognition, University of Bristol, University Walk, UK.

Abstract

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.

PMID:
9731771
DOI:
10.1038/1816
[Indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Nature Publishing Group
    Loading ...
    Support Center