Expression, purification, crystallization and preliminary X-ray diffraction analysis of nurse shark ß2-microglobulin.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 4): 460-3, 2012 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-22505420
ABSTRACT
ß(2)-Microglobulin (ß(2)m) is an essential subunit of the major histocompatibility complex (MHC) class I molecule that helps to stabilize the structure of peptide-MHC I (pMHC I). It is also one of the typical immunoglobulin superfamily (IgSF) molecules in the adaptive immune system (AIS). Sharks belong to the cartilaginous fish, which are the oldest jawed vertebrate ancestors with an AIS to exist in the world. Thus, the study of cartilaginous fish ß(2)m would help in understanding the evolution of IgSF molecules. In order to demonstrate this, ß(2)m from a cartilaginous fish, nurse shark (Ginglymostoma cirratum), was expressed, refolded, purified and crystallized. Diffraction data were collected to a resolution of 2.3 Å. The crystal belonged to space group P3(2)21, with unit-cell parameters a = b = 88.230, c = 67.146 Å. The crystal structure contained two molecules in the asymmetric unit. The results will provide structural information for study of the evolution of ß(2)m and IgSF in the AIS.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Tubarões
/
Microglobulina beta-2
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article