Structural Biology of the Complement System

Of recent, the structure of the complement system has received considerable attention, including the publication of several three-dimensional structures of complement proteins. This has led to the need for an authoritative resource to provide a complete overview of the basics, as well as an explanation of the cutting-edge work being accomplished in this emerging science. Structural Biology of the Complement System is devoted to the full exploration of structural aspects of the complement system, with special consideration of the links between molecular structure and function. Containing the work of leading authorities across the disciplines of immunology and structural biology, the book serves both as an introductory volume for newcomers to the field and as a comprehensive reference for established researchers, in particular those whose goal is the discovery of anticomplement drugs. Written in a didactic style, this volume is an appropriate resource for students in the fields of immunology and structural biology. Structural Biology of the Complement System comes with downloadable resources containing color figures, a molecular structure visualization program, and files with three-dimensional coordinates of the structures described in the book. These tools allow readers to perform tailored structural manipulation and analysis, while also serving as a starting point for further research.

Table of Contents:
The Building Blocks of the Complement System. Complement Control Protein Modules in Regulators of Complement Activation. The Classical Pathway to C1 Complex. Factors D and B: Substrate-Inducible Serine Proteases of the Alternative Pathway of Complement Activation. The Structures of Human Complement Fragments C3d and C4Ad and the Functional Insights that They Have Provided. Complement Receptor CR2/CD21 and CR2-C3d Complexes. Structure of the Anaphylatoxins C3a and C5a. C3b/C4b Binding Site of Complement Receptor Type 1 (CR1, CD35). From Structure to Function of a Complement Regulator: Decay-Accelerating Factor (CD55). Complement Protein C8. Structure-Function Relationships in CD59. Complement-Like Repeats in Proteins of the Complement System. Complement and Immunoglobulin Protein Structures by X-Ray and Neutron Solution Scattering and Analytical Ultracentrifugation. Structure, Dynamics, Activity, and Function of Compstatin and Design of More Potent Analogues. Discovery of Potent Cyclic Antagonists of Human C5a Receptors. Index.

About the Author :
Dimitrios Morikis received his B.S. in physics from Aristotle University of Thessaloniki, Greece, in 1983, and his M.S. and Ph.D. in physics from Northeastern University, Boston, in 1985 and 1990, respectively. He was trained in biophysics during his doctoral thesis work, in structural biology during his postdoctoral fellowship in 1990–1993 at the Department of Molecular Biology of The Scripps Research Institute, La Jolla, California, and in computational chemistry during a senior postdoctoral fellowship in 1999–2001 at the Department of Chemistry and Biochemistry of the University of California, San Diego. He is currently a member of the research faculty of the Department of Chemical and Environmental Engineering at the University of California, Riverside. He is also an adjunct associate professor at the Division of Immunology and the Department of Neurobiochemistry of the Beckman Research Institute of the City of Hope, Duarte, California. His research is highly cross-disciplinary, using experimental spectroscopic methods and theoretical computational methods. His current research focuses on immunophysics, structural bioinformatics, bioengineering, and biotechnology, including three-dimensional structure determination, the exploration of structure, dynamics, thermodynamics, and electrostatics of proteins and protein complexes of the immune system, rational drug design, and the design of peptides and small proteins with desired properties. John D. Lambris received his Ph.D. in biochemistry in 1979. He is a professor in the Department of Pathology and Laboratory Medicine, and director of the Protein Chemistry Laboratory at the University of Pennsylvania, Philadelphia. Using complement as a model system, he applies ideas and methods embodied in engineering, computer science, physics, chemistry, biomedicine, and other fields to study the structure and functions of the complement system. His current research efforts focus on the structural–functional aspects of protein–protein interactions, and the rational design of small size–complement inhibitors. In addition, his research extends to the evolution and developmental aspects of the complement system as well as to viral molecular mimicry and immune evasion strategies.

Review :
"…This is a unique book that offers information about what is currently known about the structure-function relationship of the complement system components. For researchers with an interest in this particular area, it would be an excellent source of information." -Doody's Review Services