3QDA

Crystal structure of W95L beta-2 microglobulin

Summary for 3QDA

• Entry DOI: 10.2210/pdb3qda/pdb
• Descriptor: Beta-2-microglobulin, TRIETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: tryptophan, immunoglobin, beta-sandwich, hydrophobic pocket, amyloidosis, dra, mhc class i, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P61769
• Total number of polymer chains: 1
• Total formula weight: 11956.48

Authors

Ricagno, S.,Bellotti, V.,Bolognesi, M. (deposition date: 2011-01-18, release date: 2011-06-29, Last modification date: 2024-11-20)

Primary citation

Raimondi, S.,Barbarini, N.,Mangione, P.,Esposito, G.,Ricagno, S.,Bolognesi, M.,Zorzoli, I.,Marchese, L.,Soria, C.,Bellazzi, R.,Monti, M.,Stoppini, M.,Stefanelli, M.,Magni, P.,Bellotti, V.
The two tryptophans of beta2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure.
BMC Evol Biol, 11:159-159, 2011

PubMed Abstract: We have recently discovered that the two tryptophans of human β2-microglobulin have distinctive roles within the structure and function of the protein. Deeply buried in the core, Trp95 is essential for folding stability, whereas Trp60, which is solvent-exposed, plays a crucial role in promoting the binding of β2-microglobulin to the heavy chain of the class I major histocompatibility complex (MHCI). We have previously shown that the thermodynamic disadvantage of having Trp60 exposed on the surface is counter-balanced by the perfect fit between it and a cavity within the MHCI heavy chain that contributes significantly to the functional stabilization of the MHCI. Therefore, based on the peculiar differences of the two tryptophans, we have analysed the evolution of β2-microglobulin with respect to these residues.

PubMed: 21663612
DOI: 10.1186/1471-2148-11-159

Experimental method

X-RAY DIFFRACTION (1.57 Å)