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Molecular Modeling of the Class I Human Histocompatibility Molecule HLA‐A2 Presenting an Allele‐Specific Nonapeptide from Influenza Matrix Protein
Author(s) -
Zimmermann Norbert,
Rötzschke Olaf,
Falk Kirsten,
Rognan Didier,
Folkers Gerd,
Rammensee HansGeorg,
Jung Günther
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199208861
Subject(s) - human leukocyte antigen , major histocompatibility complex , histocompatibility , peptide , molecular model , biology , genetics , allele , antigen , computational biology , chemistry , microbiology and biotechnology , gene , biochemistry
The conformation is not α‐helical, but extended when the antigenic peptide binds in the pocket of the human major histocompatibility complex (MHC) protein HLA‐A2 of class I. This was established by molecular modeling studies and molecular dynamics simulations on a complex of HLA‐A2 and one nonapeptide from the influenza matrix protein. The investigations are based on the structure of HLA‐A2 determined by X‐ray crystallography and the recently determined HLA‐A2‐specific peptide binding motif. The described model supports the present ideas about MHC‐limited antigenic binding.