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| PROMINENT ROLE OF SECONDARY ANCHOR RESIDUES IN PEPTIDE BINDING TO HLA-A2.1 MOLECULES |
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| Author(s): RUPPERT J, SIDNEY J, CELIS E, KUBO RT, GREY HM, SETTE A |
| Source: CELL Volume: 74 Issue: 5 Pages: 929-937 Published: SEP 10 1993 |
| Times Cited: 527 References: 26 |
| Abstract: The functional determinants of histocompatibility leukocyte antigen (HLA)-A2.1-peptide interactions have been detailed by the use of quantitative molecular binding assays and a chemically synthesized library of naturally occurring epitopes. The importance of hydrophobic anchor residues in position 2 and the C-terminus minus was confirmed. These anchors are necessary, but not sufficient, for high affinity binding, as the predictions based solely on these anchors are only about 30% accurate. Prominent roles for several other positions (1, 3, and 7) were also demonstrated. The location of these residues within the peptides matches secondary A2.1 pockets previously demonstrated by X-ray crystallography. From a functional standpoint, similar dominant negative effects on binding were observed for charged residues in both nonamers and decamers, while positive effects differed between nonamers and decamers. An extended motif taking into account secondary anchors increased the predictability of A2.1-binding epitopes to a level of 70%, underscoring the practical usefulness of extended motifs. |
| Document Type: Article |
| Language: English |
| Reprint Address: RUPPERT, J (reprint author), CYTEL CORP, 3525 JOHN HOPKINS COURT, SAN DIEGO, CA 92121 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: LX292 |
| ISSN: 0092-8674 |
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