3O81

Beta2-microglobulin from Gallus gallus

Summary for 3O81

• Entry DOI: 10.2210/pdb3o81/pdb
• Related: 1BMG 1LDS 3BEV 3BEW 3GBL
• Descriptor: Beta-2-microglobulin (2 entities in total)
• Functional Keywords: ig-like c1-type (immunoglobulin-like) domain, histocompatibility antigen, mhc class i molecule from b21 chicken, immune system
• Biological source: Gallus gallus (chickens)
• Cellular location: Secreted: P21611
• Total number of polymer chains: 2
• Total formula weight: 26109.79

Authors

Loll, B.,Hee, C.S.,Uchanska-Ziegler, B.,Ziegler, A. (deposition date: 2010-08-02, release date: 2011-08-03, Last modification date: 2024-10-30)

Primary citation

Hee, C.S.,Fabian, H.,Uchanska-Ziegler, B.,Ziegler, A.,Loll, B.
Comparative biophysical characterization of chicken beta2-microglobulin.
Biophys.Chem., 167:26-35, 2012

PubMed Abstract: β(2)-microglobulin (β(2)m) is the smallest building block of molecules belonging to the immunoglobulin superfamily. By comparing thermodynamic and structural characteristics of chicken β(2)m with those of other species, we seek to elucidate whether it is possible to pinpoint features that set the avian protein apart from other β(2)m. The thermodynamic assays revealed that chicken β(2)m exhibits a lower melting temperature than human β(2)m, and the H/D exchange behavior observed by infrared spectroscopy indicates a more flexible structure of the former protein. To understand these differences at a molecular level, we determined the structure of free chicken β(2)m by X-ray crystallography to a resolution of 2.0 Å. Our comparisons indicate that certain biophysical characteristics of the chicken protein, particularly its conformational flexibility, diverge considerably from those of the other β(2)m analyzed, although basic structural features have been retained through evolution.

PubMed: 22695053
DOI: 10.1016/j.bpc.2012.04.001

Experimental method

X-RAY DIFFRACTION (2 Å)