1jml
From Proteopedia
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|PDB= 1jml |SIZE=350|CAPTION= <scene name='initialview01'>1jml</scene>, resolution 1.90Å | |PDB= 1jml |SIZE=350|CAPTION= <scene name='initialview01'>1jml</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1hz6|1hz6]], [[1hz5|1hz5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jml OCA], [http://www.ebi.ac.uk/pdbsum/1jml PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jml RCSB]</span> | ||
}} | }} | ||
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[[Category: Neill, J W.O.]] | [[Category: Neill, J W.O.]] | ||
[[Category: Zhang, K Y.J.]] | [[Category: Zhang, K Y.J.]] | ||
| - | [[Category: ZN]] | ||
[[Category: carboxy-terminal beta-strand swapped.]] | [[Category: carboxy-terminal beta-strand swapped.]] | ||
[[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]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:48 2008'' |
Revision as of 18:35, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 1hz6, 1hz5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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