The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
The human major histocompatibility complex class Ib molecule HLA‐E binds signal sequence‐derived peptides with primary anchor residues at positions 2 and 9
Abstract
Human histocompatibility leukocyte antigen E (HLA‐E) and mouse major histocompatibility complex (MHC) class Ib antigen, Qa‐1, share the same substitutions at two normally conserved positions 143 and 147, which are likely to affect binding of the C terminus of peptides. Qa‐1 is able to bind a peptide derived from the leader sequence of H‐2 D and H‐2 L molecules. We developed a peptide binding assay in vitro to compare the binding specificity of HLA‐E with the mouse MHC class Ib molecule Qa‐1. We demonstrate that HLA‐E binds, although poorly, the peptide which binds to Qa‐1 and that it also binds nonamer signal sequence‐derived peptides from human MHC class I molecules. Using alanine and glycine substitutions, we could define primary anchor residues at positions 2 and 9 and secondary anchor residues at position 7 and possibly 3.
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Cited by
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Association of DAP12 with Activating CD94/NKG2C NK Cell Receptors
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Metadata
- Authors
- Braud, V., Yvonne Jones, E., & McMichael, A.
- Venue
- European Journal of Immunology
- Publisher
- Wiley
- Published
- 1997-05
- Volume
- 27
- Issue
- 5
- Pages
- 1164-1169
- ISSN
- 0014-2980 (ISSN-L)
- 1521-4141
- OpenAlex
- W1964653209
- Cited by
- 502
- References
- 22
- FWCI
- 11.47
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: The human major histocompatibility complex class Ib molecule HLA‐E binds signal sequence‐derived peptides with primary anchor residues at positions 2 and 9. https://app.cochat.ai/papers/10.1002/eji.1830270517
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- Braud, V., Yvonne Jones, E., & McMichael, A. (1997). The human major histocompatibility complex class Ib molecule HLA‐E binds signal sequence‐derived peptides with primary anchor residues at positions 2 and 9. European Journal of Immunology. https://doi.org/10.1002/eji.1830270517
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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