Members of the regulator of complement activation (RCA) protein family perform a vital role in health and disease. In this report we describe our efforts to solve the structures of human membrane cofactor protein (CD46), the vaccinia virus complement control protein, which mimics mammalian RCA proteins, and human complement receptor type 1 (CD35). These examples illustrate that, despite good progress over the last decade, the regulators of complement, as extracellular multiple domain glycoproteins, still pose formidable problems to structural biologists. Many important questions remain unanswered, in particular with regard to the flexibility of these proteins and the extent to which they undergo conformational rearrangements on engaging their binding partners
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November 2002
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Conference Article|
November 01 2002
Three-dimensional structure and flexibility of proteins of the RCA family — a progress report
A. Herbert;
A. Herbert
*Department of Chemistry, University of Edinburgh, Edinburgh EH9 3JJ, U.K.
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J. O'Leary;
J. O'Leary
†Department of Biochemistry, University of Oxford, Oxford OX1 4QY, U.K.
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M. Krych-Goldberg;
M. Krych-Goldberg
‡Division of Rheumatology, Department of Medicine, Washington university School of Medicine, St. Louis, MO 63110, U.S.A.
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J. P. Atkinson;
J. P. Atkinson
‡Division of Rheumatology, Department of Medicine, Washington university School of Medicine, St. Louis, MO 63110, U.S.A.
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P. N. Barlow
P. N. Barlow
1
*Department of Chemistry, University of Edinburgh, Edinburgh EH9 3JJ, U.K.
1To whom correspondence should be addressed (e-mail Paul.Barlowa@ac.uk)
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Publisher: Portland Press Ltd
Received:
June 18 2002
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2002 Biochemical Society
2002
Biochem Soc Trans (2002) 30 (6): 990–996.
Article history
Received:
June 18 2002
Citation
A. Herbert, J. O'Leary, M. Krych-Goldberg, J. P. Atkinson, P. N. Barlow; Three-dimensional structure and flexibility of proteins of the RCA family — a progress report. Biochem Soc Trans 1 November 2002; 30 (6): 990–996. doi: https://doi.org/10.1042/bst0300990
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