Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10687-91. Epub 2001 Aug 28.

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

Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D.

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Department of Biochemistry and Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA.

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Proc Natl Acad Sci U S A 2002 May 28;99(11):7809.

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.

PMID:: 11526208; [PubMed - indexed for MEDLINE]
PMCID: PMC58527

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Structures reported by this article

Conversion Of Monomeric Protein L To An Obligate Dimer By Computational Protein Design

PDB: 1JML

Source: Finegoldia magna

Method: X-Ray Diffraction

Resolution: 1.9 Å

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