1jml
From Proteopedia
(New page: 200px<br /><applet load="1jml" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jml, resolution 1.90Å" /> '''Conversion of Monome...) |
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| - | [[Image:1jml.jpg|left|200px]]<br /><applet load="1jml" size=" | + | [[Image:1jml.jpg|left|200px]]<br /><applet load="1jml" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jml, resolution 1.90Å" /> | caption="1jml, resolution 1.90Å" /> | ||
'''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design'''<br /> | '''Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Protein L consists of a single alpha-helix packed on a four-stranded | + | 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== | ==About this Structure== | ||
| - | 1JML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JML is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JML OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Baker, D.]] | [[Category: Baker, D.]] | ||
| - | [[Category: Kim, D | + | [[Category: Kim, D E.]] |
[[Category: Kuhlman, B]] | [[Category: Kuhlman, B]] | ||
| - | [[Category: Neill, J | + | [[Category: Neill, J W.O.]] |
| - | [[Category: Zhang, K | + | [[Category: Zhang, K Y.J.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: carboxy-terminal beta-strand swapped.]] | [[Category: carboxy-terminal beta-strand swapped.]] | ||
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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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:21 2008'' |
Revision as of 11:24, 21 February 2008
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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 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
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