1jml
From Proteopedia
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[[Image:1jml.jpg|left|200px]] | [[Image:1jml.jpg|left|200px]] | ||
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'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design''' | '''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design''' | ||
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[[Category: Neill, J W.O.]] | [[Category: Neill, J W.O.]] | ||
[[Category: Zhang, K Y.J.]] | [[Category: Zhang, K Y.J.]] | ||
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| - | [[Category: | + | [[Category: Domain swapped dimer]] |
| - | [[Category: | + | [[Category: Four stranded beta-sheet with central alpha helix]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:24:57 2008'' | |
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Revision as of 18:24, 2 May 2008
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. 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 Fri May 2 21:24:57 2008
