Molecular Modeling of the Class I Human Histocompatibility Molecule HLA‐A2 Presenting an Allele‐Specific Nonapeptide from Influenza Matrix Protein

N Zimmermann, O Rötzschke, K Falk… - … Edition in English, 1992 - Wiley Online Library
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 …

Molecular dynamics study of a complex between the human histocompatibility antigen HLA‐A2 and the IMP58‐66 nonapeptide from influenza virus matrix protein

D Rognan, N ZIMMERMANN, G Jung… - European journal of …, 1992 - Wiley Online Library
The structure of the influenza‐virus‐matrix‐protein (IMP) 58‐66 nonapeptide, bound to the
major‐histocompatibility‐complex‐encoded human leukocyte antigen (HLA) A2 protein was …

Crystal structures of HLA‐A* 0201 complexed with antigenic peptides with either the amino‐or carboxyl‐terminal group substituted by a methyl group

M Bouvier, HC Guo, KJ Smith… - … : Structure, Function, and …, 1998 - Wiley Online Library
The crystal structures of class I major histocompatibility complex (MHC) molecules
complexed with antigenic peptides revealed a network of hydrogen bonds between the …

A model of water structure inside the HLA-A2 peptide binding groove.

WS Meng, H von Grafenstein… - International …, 1997 - academic.oup.com
Based on molecular dynamics simulations, it is proposed that water within the binding
groove of the human MHC class I molecule HLA-A2 plays a role in the formation of its …

Changes at the floor of the peptide‐binding groove induce a strong preference for Proline at position 3 of the bound peptide: Molecular dynamics simulations of HLA …

H Toh, CJ Savoie, N Kamikawaji, S Muta… - Biopolymers …, 2000 - Wiley Online Library
We report on molecular dynamics simulations of major histocompatibility complex (MHC)–
peptide complexes. Class I MHC molecules play an important role in cellular immunity by …

Both major and minor peptide-binding pockets in HLA-A2 influence the presentation of influenza virus matrix peptide to cytotoxic T lymphocytes

JMC Teng, KT Hogan - Molecular immunology, 1994 - Elsevier
Most of the polymorphic residues in class I MHC molecules are concentrated in the α 1-and
α2-domains with their side chains pointing towards the antigen peptide site. Previous crystal …

Selection of peptides that bind to the HLA-A2. 1 molecule by molecular modelling

JS Lim, S Kim, HG Lee, KY Lee, TJ Kwon, K Kim - Molecular immunology, 1996 - Elsevier
Cytotoxic T lymphocytes recognize antigenic peptides in association with major
histocompatibility complex class I proteins. Although a large set of class I binding peptides …

Crystal structures of two peptide–HLA-B* 1501 complexes; structural characterization of the HLA-B62 supertype

G Røder, T Blicher, S Justesen… - … Section D: Biological …, 2006 - journals.iucr.org
MHC class I molecules govern human cytotoxic T cell responses. Their specificity
determines which peptides they sample from the intracellular protein environment and then …

Fine specificity of antigen binding to two class I major histocompatibility proteins (B* 2705 and B* 2703) differing in a single amino acid residue

D Rognan, S Krebs, O Kuonen, JR Lamas… - Journal of computer …, 1997 - Springer
Starting from the X-ray structure of a class I majorhistocompatibility complex (MHC)-encoded
protein (HLA-B* 2705), a naturallypresented self-nonapeptide and two synthetic analogues …

Rational design of nonnatural peptides as high-affinity ligands for the HLA-B* 2705 human leukocyte antigen.

D Rognan, L Scapozza, G Folkers… - Proceedings of the …, 1995 - National Acad Sciences
From the three-dimensional structure of the class I major histocompatibility complex (MHC)
HLA-B* 2705 protein, several nonnatural peptides were designed either to optimize the …