This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 14: | Line 14: | ||
[[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.]] | ||
| Line 23: | Line 23: | ||
[[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
|
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
Page seeded by OCA on Thu Feb 21 13:24:21 2008
