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Protein Pept Lett. 2007;14(9):903-16.

Robust quantitative modeling of peptide binding affinities for MHC molecules using physical-chemical descriptors.

Author information

1
Sealy Center for Structural Biology and Molecular Biophysics, Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, 301 University Boulevard, Galveston, Texas 77555-0857, USA.

Abstract

Major histocompatibility complex (MHC) molecules bind short peptides resulting from intracellular processing of foreign and self proteins, and present them on the cell surface for recognition by T-cell receptors. We propose a new robust approach to quantitatively model the binding affinities of MHC molecules by quantitative structure-activity relationships (QSAR) that use the physical-chemical amino acid descriptors E1-E5. These QSAR models are robust, sequence-based, and can be used as a fast and reliable filter to predict the MHC binding affinity for large protein databases.

PMID:
18045233
PMCID:
PMC2643840
[Indexed for MEDLINE]
Free PMC Article

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