3lve
LEN Q38E MUTANT: A DOMAIN FLIP FROM A SINGLE AMINO ACID SUBSTITUTION
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OverviewOverview
BACKGROUND: 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. RESULTS:, Single-site mutants of light-chain variable domain Len, designated LenQ38E, and LenK30T, formed 'flipped' dimers in which one domain was rotated by, about 180 degrees compared with the native protein. The dimer in the, native protein is similar to that found between variable domains in Fab, immunoglobulin fragments. When compared to the native dimer, more surface, area is ... [(full description)]
About this StructureAbout this Structure
3LVE is a [Single protein] structure of sequence from [Homo sapiens] with ZN as [ligand]. Structure known Active Site: ZNB. Full crystallographic information is available from [OCA].
ReferenceReference
A domain flip as a result of a single amino-acid substitution., Pokkuluri PR, Huang DB, Raffen R, Cai X, Johnson G, Stevens PW, Stevens FJ, Schiffer M, Structure. 1998 Aug 15;6(8):1067-73. PMID:9739086
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