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

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Design of new small cyclic melanocortin receptor-binding peptides using molecular modelling: Role of the His residue in the melanocortin peptide core.

The conserved core of melanocyte stimulating hormones (MSH), His-Phe-Arg-Trp, was probed by comparing a cyclic pentapeptide containing His-DPhe-Arg-Trp, with three structurally similar cyclic peptides, that lacked the His residue. All three peptides bound to the MC(1), MC(3), MC(4) and MC(5) receptors with similar affinities. Molecular modelling indicated that the 3D structure of the DPhe-Arg-Trp of all three peptides were closely similar. The data indicate that the His residue of the small rigid cyclic MSH core peptides does not participate in binding with the melanocortin receptors.[1]

References

  1. Design of new small cyclic melanocortin receptor-binding peptides using molecular modelling: Role of the His residue in the melanocortin peptide core. Prusis, P., Muceniece, R., Mutule, I., Mutulis, F., Wikberg, J.E. European journal of medicinal chemistry. (2001) [Pubmed]
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