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The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure

Raimondi, S; Barbarini, N; Mangione, P; Esposito, G; Ricagno, S; Bolognesi, M; Zorzoli, I; ... Bellotti, V; + view all (2011) The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure. BMC Evolutionary Biology , 11 (June 2) , Article 159. 10.1186/1471-2148-11-159. Green open access

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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.

Type: Article
Title: The two tryptophans of β2-microglobulin have distinct roles in function and folding and might represent two independent responses to evolutionary pressure
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1186/1471-2148-11-159
Publisher version: http://dx.doi.org/10.1186/1471-2148-11-159
Language: English
Additional information: PMCID: PMC3124429 © 2011 Raimondi et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Keywords: Amino Acid Sequence, Amyloid, Animals, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Folding, Sequence Alignment, Tryptophan, beta 2-Microglobulin
UCL classification: UCL
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Inflammation
URI: https://discovery.ucl.ac.uk/id/eprint/1356160
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