Abstract
Complement control protein (CCP) modules, or short consensus repeats (SCR), exist in a wide variety of complement and adhesion proteins, principally the selectins. We have predicted the three-dimensional structure of a CCP module based upon secondary structural information derived by two-dimensional NMR [Barlow et al. (1991), Biochemistry 30, 997–1004]. Accordingly, the CCP is predicted to contain seven β-strands with extensive hydrogen-bonding interactions, and shows a compact, globular structure. Comparison of this model to the X-ray structure of a kringle domain suggests that the CCP unit is more compact than a kringle structure, and that despite their similarities in size and disulfide bond format, the two are not homologous. Although the function of CCP domains is unknown, it is hoped that the structural model presented herein will facilitate further inquiry into how they contribute to so many systems of biological importance.
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Chou, KC., Heinrikson, R.L. Prediction of the Tertiary Structure of the Complement Control Protein Module. J Protein Chem 16, 765–773 (1997). https://doi.org/10.1023/A:1026363816730
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DOI: https://doi.org/10.1023/A:1026363816730