Prediction of the tertiary structure of the complement control protein module

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...

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Bibliographic Details
Published in:Journal of Protein Chemistry 1997-11, Vol.16 (8), p.765-773
Main Authors: Chou, K C, Heinrikson, R L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biochemistry
Complement
Complement System Proteins - chemistry
Computer Graphics
Crystallography, X-Ray
Disulfides - metabolism
Humans
Hydrogen Bonding
Models, Structural
Modules
Molecular biology
Molecular Sequence Data
NMR
Nuclear magnetic resonance
Protein Conformation
Protein Folding
Protein structure
Protein Structure, Tertiary
Proteins
Selectins
Selectins - chemistry
Structural models
Tertiary structure
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Summary: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 beta-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.
ISSN:0277-8033
1572-3887
1573-4943
DOI:10.1023/a:1026363816730