ArticleProtein science : a publication of the Protein Society2004
Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Seizure-Related Homolog Protein 6 (SEZ6): Biology and Therapeutic Target in Neuroendocrine Carcinomas.Clinical cancer research : an official journal of the American Association for Cancer Research · 2025Review
- Structural biology of complement receptors.Frontiers in immunology · 2023Review
- Sushi-Repeat-Containing Protein X-Linked 2: A Potential Therapeutic Target for Inflammation and Cancer Therapy.Journal of immunology research · 2022Review
- Cardiolipin interacts with beta-2-glycoprotein I and forms an open conformation-Mechanisms analyzed using hydrogen/deuterium exchange.Protein science : a publication of the Protein Society · 2021Article
- The Sez6 Family Inhibits Complement by Facilitating Factor I Cleavage of C3b and Accelerating the Decay of C3 Convertases.Frontiers in immunology · 2021Article
- High SRPX2 protein expression predicts unfavorable clinical outcome in patients with prostate cancer.OncoTargets and therapy · 2018Article
- Comparative analyses of glycerotoxin expression unveil a novel structural organization of the bloodworm venom system.BMC evolutionary biology · 2017Article
- SRPX2 Enhances the Epithelial-Mesenchymal Transition and Temozolomide Resistance in Glioblastoma Cells.Cellular and molecular neurobiology · 2016Article
- SRPX2 is a novel chondroitin sulfate proteoglycan that is overexpressed in gastrointestinal cancer.PloS one · 2012Article
- Identification, characterization and antigenicity of the Plasmodium vivax rhoptry neck protein 1 (PvRON1).Malaria journal · 2011Article
- Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Immunophysical properties and prediction of activities for vaccinia virus complement control protein and smallpox inhibitor of complement enzymes using molecular dynamics and electrostatics.Biophysical journal · 2006Article
- Localization of regions in CD46 that interact with adenovirus.Journal of virology · 2005Article
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10 authors.
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Abstract
The regulators of complement activation (RCA) are critical to health and disease because their role is to ensure that a complement-mediated immune response to infection is proportionate and targeted. Each protein contains an uninterrupted array of from four to 30 examples of the very widely occurring complement control protein (CCP, or sushi) module. The CCP modules mediate specific protein-protein and protein-carbohydrate interactions that are key to the biological function of the RCA and, paradoxically, provide binding sites for numerous pathogens. Although structural and mutagenesis studies of CCP modules have addressed some aspects of molecular recognition, there have been no studies of the role of molecular dynamics in the interaction of CCP modules with their binding partners. NMR has now been used in the first full characterization of the backbone dynamics of CCP modules. The dynamics of two individual modules-the 16th of the 30 modules of complement receptor type 1 (CD35), and the N-terminal module of membrane cofactor protein (CD46)-as well as their solution structures, are compared. Although both examples share broadly similar three-dimensional structures, many structurally equivalent residues exhibit different amplitudes and timescales of local backbone motion. In each case, however, regions of the module-surface implicated by mutagenesis as sites of interactions with other proteins include several mobile residues. This observation suggests further experiments to explore binding mechanisms and identify new binding sites.
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