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. 1993 Aug 15;90(16):7686–7690. doi: 10.1073/pnas.90.16.7686

Amino acid residues essential for biological activity of a peptide derived from a major histocompatibility complex class I antigen.

J Stagsted 1, C Mapelli 1, C Meyers 1, B W Matthews 1, C B Anfinsen 1, A Goldstein 1, L Olsson 1
PMCID: PMC47207  PMID: 8356070

Abstract

The stimulatory activity of peptides from the alpha 1 domain of the major histocompatibility complex (MHC) class I antigen on adipose cell glucose transport was previously shown to require a preformed, ordered conformation of the peptide. The two peptides studied previously were Dk-(61-85) (ERETQIAKGNEQSFRVDLRTLLRYY) and Dk-(69-85). We now show that systematic alanine substitution in Dk-(69-85) identifies residues that are essential for biological activity. Ordered structure of the peptides, estimated by circular dichroism, was found in all peptides with activity, but with a complex variety of spectra. Inactive peptides were in either a random coil or an ordered structure. Ordered structure, therefore, is not sufficient for activity. The peptides self-interact in the absence of cells and form aggregates that precipitate upon centrifugation. The tendency to aggregate is correlated with biological potency. Only MHC class I molecules have significant homology to the peptides studied here. The peptide self-interaction suggests that the biological effects in cells, which result from inhibition of receptor and transporter internalization, may be due to the binding (tantamount to self-interaction) of the peptide to the homologous sequences in the alpha 1 domain of the MHC class I molecule.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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