Published January 1, 2005
| public
Journal Article
Pillars Article: Structure of the human class I histocompatibility antigen, HLA-A2
Abstract
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel {3-strands topped by a-helices. A large groove between the a-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.
Additional Information
© 2005 American Association of Immunologists. We thank Anastasia Haykov for excellent technical assistance; Hans Bartunik and Klaus Bartels, Keith Moffat and Wilfried Schildkamp and Paul Phizackerley for help with synchrotron data collection, Mike Silver and Tom Garrett for help with the figures and our colleagues in the structural molecular biology group. We also thank Drs Dean Mann (NIH), D. Michael Strong and James Woody (U.S. Naval Research Unit) and Don Giard (MIT Cell Culture Facility) for provision of cells which made this work possible. B.S. thanks the Algerian Ministere de l'Enseignment et de la Recherche Scientifique for a postdoctoral leave. P.J.B. held an American Cancer Society postdoctoral fellowship during part of the work. The research was supported by the NIH and the Howard Hughes Medical Institute.Additional details
- Eprint ID
- 75429
- Resolver ID
- CaltechAUTHORS:20170327-140247273
- NIH
- Howard Hughes Medical Institute (HHMI)
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2017-03-27Created from EPrint's datestamp field
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2019-10-03Created from EPrint's last_modified field