1jml: Difference between revisions
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[[Image:1jml.jpg|left|200px]] | [[Image:1jml.jpg|left|200px]] | ||
'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design''' | {{Structure | ||
|PDB= 1jml |SIZE=350|CAPTION= <scene name='initialview01'>1jml</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JML is a [ | 1JML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11526208 11526208] | ||
[[Category: Finegoldia magna]] | [[Category: Finegoldia magna]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four stranded beta-sheet with central alpha helix]] | [[Category: four stranded beta-sheet with central alpha helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:27 2008'' | ||
Revision as of 10:05, 20 March 2008
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| 1jml, resolution 1.90Å | |||||||||||||
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| Ligands: | ZN | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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
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