Barbara Curli, Italiane al lavoro, 1914–1920, Marsilio, Venice, 1998, 338 pp., ISBN 88-317-6938-3 pbk, 49,000 Lire

Willson, Perry

doi:10.1017/s1353294400007869

Modern Italy

2000

DOI: 10.1017/s1353294400007869

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Barbara Curli, Italiane al lavoro, 1914–1920, Marsilio, Venice, 1998, 338 pp., ISBN 88-317-6938-3 pbk, 49,000 Lire

Perry Willson

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“…Nevertheless, despite these restrictions, some longer peptides can bind to MHC-I (23)(24)(25)(26)(27)(28)(29). These longer epitopes can either extend beyond the conventional C-terminal anchor site (29,30) or bulge centrally from the antigen-binding cleft (25,28,31). An extreme example of accommodating a lengthy class I-restricted peptide was observed in rat MHC-I RT1-A a complexed to a 13-mer epitope, MTF-E (25).…”

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confidence: 99%

High Resolution Structures of Highly Bulged Viral Epitopes Bound to Major Histocompatibility Complex Class I

Tynan

Borg

Miles

et al. 2005

Journal of Biological Chemistry

151

163

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mentioning

confidence: 99%

High Resolution Structures of Highly Bulged Viral Epitopes Bound to Major Histocompatibility Complex Class I

Tynan

Borg

Miles

et al. 2005

Journal of Biological Chemistry

151

163

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“…Structural studies of human and murine MHC class I proteins in complex with a variety of peptides have revealed conservative structural elements that promote efficient binding and presentation of peptide epitopes (5)(6)(7)(8)(9). Peptides of 8 -10 residues are bound in a predominantly extended conformation within a narrow groove formed by two antiparallel ␣-helices positioned above an eight-strand ␤-sheet platform.…”

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confidence: 99%

Structural Definition of the H-2Kd Peptide-binding Motif

Mitaksov

Fremont

2006

Journal of Biological Chemistry

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Classic major histocompatibility complex (MHC) proteins associate with antigen-and self-derived peptides in an allele-specific manner. Herein we present the crystal structure of the MHC class I protein H-2K d (K d ) expressed by BALB/c mice in complex with an antigenic peptide derived from influenza A/PR/8/34 nucleoprotein (Flu, residues 147-155, TYQRTRALV). Analysis of our structure in conjunction with the sequences of naturally processed epitopes provides a comprehensive understanding of the dominant K d peptide-binding motif. We find that Flu residues Tyr P2 , Thr P5 , and Val P9 are sequestered into the B, C, and F pockets of the K d groove, respectively. The shape and chemistry of the polymorphic B pocket make it an optimal binding site for the side chain of Tyr P2 as the dominant anchoring residue of nonameric peptides. The non-polar F pocket limits the amino acid repertoire at P9 to hydrophobic residues such as Ile, Leu, or Val, whereas the C pocket restricts the size of the P5-anchoring side chain. We also show that Flu is accommodated in the complex through an unfavorable kink in the otherwise extended peptide backbone due to the presence of a prominent ridge in the K d groove. Surprisingly, this backbone conformation is strikingly similar to D b -presented peptides despite the fact that these proteins employ distinct motif-anchoring strategies. The results presented in this study provide a solid foundation for the understanding of K d -restricted antigen presentation and recognition events.Class I major histocompatibility complex (MHC) 2 proteins serve a critical role in the adaptive immune response by binding short peptide fragments intracellularly and presenting them at the cell surface for surveillance by cytotoxic T lymphocytes (1-4). Structural studies of human and murine MHC class I proteins in complex with a variety of peptides have revealed conservative structural elements that promote efficient binding and presentation of peptide epitopes (5-9). Peptides of 8 -10 residues are bound in a predominantly extended conformation within a narrow groove formed by two antiparallel ␣-helices positioned above an eight-strand ␤-sheet platform. Conservative hydrogen bonding networks are established in the binding groove with peptide mainchain and terminal atoms that enable largely sequence-independent ligation.Although low affinity, kinetically short-lived peptide-MHC complexes can be established by highly diverse epitope sequences, stable association requires the anchoring of peptide side chains into specific pockets in the MHC groove. MHC polymorphisms are clustered in these pockets (3, 10, 11), and their shape and chemistry impose constraints that are reflected by allele-specific motifs found in the sequences of naturally processed peptides (12, 13). For example, H-2 d cell lines (P815) and H-2 b cell lines (EL4) infected with the same influenza virus present different antigenic peptides for CTL recognition (14). Thus, outbred populations that express varied MHC proteins can survey diverse peptide fragme...

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Barbara Curli, Italiane al lavoro, 1914–1920, Marsilio, Venice, 1998, 338 pp., ISBN 88-317-6938-3 pbk, 49,000 Lire

Cited by 2 publications

References 0 publications

High Resolution Structures of Highly Bulged Viral Epitopes Bound to Major Histocompatibility Complex Class I

High Resolution Structures of Highly Bulged Viral Epitopes Bound to Major Histocompatibility Complex Class I

Structural Definition of the H-2Kd Peptide-binding Motif

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