Work

Conversion of monomeric protein L to an obligate dimer by computational protein design

Year: 2001

Type: article

Abstract: Protein L consists of a single alpha-helix packed on a four-stranded beta-sheet formed by two symmetrically opposed beta-hairpins. We use a computer-based protein design procedure to stabilize a domain-swapped dimer of protein L in which the second beta-turn straightens and the C-terminal strand inserts into the beta-sheet of the partner. The designed obligate dimer contains three mutations (A52V, N53P, and G55A) and has a dissociation constant of approximately 700 pM, which is comparable to the dissociation constant of many naturally occurring protein dimers. The structure of the dimer has been determined by x-ray crystallography and is close to the in silico model.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.181354398

Authors: Brian Kuhlman, Jason W. O'Neill, David E. Kim, Kam Y. J. Zhang, David Baker

Institutions: Howard Hughes Medical Institute, University of Washington, Fred Hutch Cancer Center

Language: English

Topic: Protein Structure and Dynamics

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

OpenAlex ID: W1975666063

FWCI: 2.095

Cites: 28

Cited by: 77

Related to: 10