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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.

The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.[1]

References

  1. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Smith, K.J., Reid, S.W., Harlos, K., McMichael, A.J., Stuart, D.I., Bell, J.I., Jones, E.Y. Immunity (1996) [Pubmed]
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