1jml

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{{STRUCTURE_1jml| PDB=1jml | SCENE= }}
{{STRUCTURE_1jml| PDB=1jml | SCENE= }}
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'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design'''
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===Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11526208 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11526208}}
==About this Structure==
==About this Structure==
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[[Category: Domain swapped dimer]]
[[Category: Domain swapped dimer]]
[[Category: Four stranded beta-sheet with central alpha helix]]
[[Category: Four stranded beta-sheet with central alpha helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:28:27 2008''

Revision as of 17:28, 1 July 2008

Image:1jml.png

Template:STRUCTURE 1jml

Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design

Template:ABSTRACT PUBMED 11526208

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

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