(Q33913099)

English

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-A*0217.

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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-A*0217. (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

Toh H

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Savoie CJ

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Kamikawaji N

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Muta S

4

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Sasazuki T

5

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Kuhara S

6

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

publication date

1 October 2000

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

54

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

5

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

318-327

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules

1 reference

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Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 A resolution

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Binding of viral antigens to major histocompatibility complex class I H-2Db molecules is controlled by dominant negative elements at peptide non-anchor residues. Implications for peptide selection and presentation.

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Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules

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A novel subtype of A2 (A*0217) isolated from the South American Indian B-cell line AMALA.

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The peptide-binding motif of HLA-A*0217.

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H-2Dd exploits a four residue peptide binding motif

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Three-dimensional structure of H-2Dd complexed with an immunodominant peptide from human immunodeficiency virus envelope glycoprotein 120

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

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

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

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

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Substituting nonpeptidic spacers for the T cell receptor-binding part of class I major histocompatibility complex-binding peptides.

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The missing term in effective pair potentials

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Solvent-accessible surfaces of proteins and nucleic acids

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The HLA-A*0207 peptide binding repertoire is limited to a subset of the A*0201 repertoire

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Thermodynamic and structural compensation in "size-switch" core repacking variants of bacteriophage T4 lysozyme

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Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding.

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Molecular modeling of hen egg lysozyme HEL[52-61] peptide binding to I-Ak MHC class II molecule

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Identifiers

10.1002/1097-0282(20001015)54:5<318::AID-BIP30>3.0.CO;2-T

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

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