4LVE

LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION

Summary for 4LVE

• Entry DOI: 10.2210/pdb4lve/pdb
• Descriptor: LEN (2 entities in total)
• Functional Keywords: immunoglobulin, kappa-iv, light chain dimer
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 25243.87

Authors

Schiffer, M.,Pokkuluri, P.R. (deposition date: 1998-05-12, release date: 1999-05-18, Last modification date: 2023-08-09)

Primary citation

Pokkuluri, P.R.,Huang, D.B.,Raffen, R.,Cai, X.,Johnson, G.,Stevens, P.W.,Stevens, F.J.,Schiffer, M.
A domain flip as a result of a single amino-acid substitution.
Structure, 6:1067-1073, 1998

PubMed Abstract: The self-assembly properties of beta domains are important features of diverse classes of proteins that include cell-adhesion molecules, surface receptors and the immunoglobulin superfamily. Immunoglobulin light-chain variable domains are well suited to the study of structural factors that determine dimerization, including how residues at the interface influence the preferred dimer arrangement.

PubMed: 9739086
DOI: 10.1016/S0969-2126(98)00107-5

Experimental method

X-RAY DIFFRACTION (2.3 Å)