MH2c: Characterization of major histocompatibility α-helices – an information criterion approach

Published: 1 July 2012| Version 1 | DOI: 10.17632/td7j6z5t37.1
B. Hischenhuber, F. Frommlet, W. Schreiner, B. Knapp


Abstract Major histocompatibility proteins share a common overall structure or peptide binding groove. Two binding groove domains, on the same chain for major histocompatibility class I or on two different chains for major histocompatibility class II, contribute to that structure that consists of two α-helices (“wall”) and a sheet of eight anti-parallel beta strands (“floor”). Apart from the peptide presented in the groove, the major histocompatibility α-helices play a central role for the interaction... Title of program: MH<sup>2</sup>c (MH helix curves) Catalogue Id: AELX_v1_0 Nature of problem Major histocompatibility (MH) proteins share a similar overall structure. However, identical MH alleles which present different peptides differ by subtle conformational alterations. One hypothesis is that such conformational differences could be another level of T cell regulation. By this software package we present a reliable and systematic way to compare different MH structures to each other. Versions of this program held in the CPC repository in Mendeley Data AELX_v1_0; MH<sup>2</sup>c (MH helix curves); 10.1016/j.cpc.2012.02.008 This program has been imported from the CPC Program Library held at Queen's University Belfast (1969-2018)



Atomic Physics, Computational Physics, Computational Method