1jml
From Proteopedia
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Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design
Overview
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.
About this Structure
1JML is a Single protein structure of sequence from Finegoldia magna with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Conversion of monomeric protein L to an obligate dimer by computational protein design., Kuhlman B, O'Neill JW, Kim DE, Zhang KY, Baker D, Proc Natl Acad Sci U S A. 2001 Sep 11;98(19):10687-91. Epub 2001 Aug 28. PMID:11526208
Page seeded by OCA on Sat Nov 24 23:52:50 2007
