1JML

Conversion of Monomeric Protein L to an Obligate Dimer by Computational Protein Design

Summary for 1JML

• Entry DOI: 10.2210/pdb1jml/pdb
• Related: 1hz5 1hz6
• Descriptor: Protein L, ZINC ION (3 entities in total)
• Functional Keywords: domain swapped dimer, four stranded beta-sheet with central alpha helix, carboxy-terminal beta-strand swapped., protein binding
• Biological source: Finegoldia magna
• Total number of polymer chains: 1
• Total formula weight: 8259.21

Authors

O'Neill, J.W.,Kuhlman, B.,Kim, D.E.,Zhang, K.Y.J.,Baker, D. (deposition date: 2001-07-19, release date: 2001-10-10, Last modification date: 2023-08-16)

Primary citation

Kuhlman, B.,O'Neill, J.W.,Kim, D.E.,Zhang, K.Y.,Baker, D.
Conversion of monomeric protein L to an obligate dimer by computational protein design.
Proc.Natl.Acad.Sci.USA, 98:10687-10691, 2001

PubMed Abstract: 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.

PubMed: 11526208
DOI: 10.1073/pnas.181354398

Experimental method

X-RAY DIFFRACTION (1.9 Å)