Characterization of the functional domain of β2-microglobulin from the Asian seabass, Lates calcarifer.

ABSTRACT:

Background

β2-Microglobulin (β(2)M) is the light chain of major histocompatibility class I (MHC I) that binds non-covalently with the α heavy chain. Both proteins attach to the antigen peptide, presenting a complex to the T cell to be destroyed via the immune mechanism.

Methodology/principal findings

In this study, a cDNA sequence encoding β(2)M in the Asian seabass (Lates calcarifer) was identified and analyzed using in silico approaches to predict and characterize its functional domain. The β(2)M cDNA contains an open reading frame (ORF) of 351 bases with a coding capacity of 116 amino acids. A large portion of the protein consists of the IG constant domain (IGc1), similar to β(2)M sequences from other species studied thus far. Alignment of the IGc1 domains of β(2)M from L

SUBMITTER: Mohd-Padil H 

PROVIDER: S-EPMC2950848 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature