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1jml

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|PDB= 1jml |SIZE=350|CAPTION= <scene name='initialview01'>1jml</scene>, resolution 1.90&Aring;
|PDB= 1jml |SIZE=350|CAPTION= <scene name='initialview01'>1jml</scene>, resolution 1.90&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:05:27 2008''
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''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


PDB ID 1jml

Drag the structure with the mouse to rotate
, 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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