Note: Front Cover -- Structural Biology in Immunology: Structure/Function of Novel Molecules of Immunologic Importance -- Copyright -- Dedication -- Contents -- Contributors -- Acknowledgments -- Chapter 1: Organization of Immunological Synapses and Kinapses -- 1.1 Introduction -- 1.2 Receptors and Ligands of the Immunological Synapse and Kinapse -- 1.2.1 T-cell Receptor and pAgMHC -- 1.2.2 Adhesion Molecules -- 1.2.3 Costimulatory and Checkpoint Receptors -- 1.2.4 Nectins and Other Adhesion Receptors -- 1.2.5 Coreceptors and Large Transmembrane Phosphatases -- 1.3 Phase-Like Behavior and Phase Separation in Signaling -- 1.3.1 Phase Separation in Adhesion Plane of Cell-Cell Interfaces -- 1.3.2 Phase-Separated Lipid Domains in Plasma Membrane -- 1.3.3 Phase Separation in Membrane Proximal Signaling -- 1.3.4 Cytoskeletal Networks -- 1.4 Microvilli/Filopodia -- 1.4.1 Rosette-Shaped Actin Network -- 1.5 Synaptic Cleft Formation -- 1.5.1 Membrane Traffic to Maintain Signaling -- 1.5.2 Extracellular Vesicles to Terminate Signaling and Relay Messages -- 1.5.3 Directed Release of Effector Molecules Through Exocytosis -- 1.6 Conclusions -- Acknowledgments -- References -- Chapter 2: Principles of Protein Recognition by Small T-Cell Adhesion Proteins and Costimulatory Receptors -- 2.1 Introduction -- 2.2 Cell-Cell Recognition and Adhesion: CD2 Family Proteins -- 2.2.1 Rat sCD2 (1992) -- 2.2.1.1 The Structure -- 2.2.1.2 What We Learnt -- 2.2.2 Human sCD2 (1994) -- 2.2.2.1 The Structure -- 2.2.2.2 What We Learnt -- 2.2.3 The Role of Charged Residues in Ligand Binding by CD2 (1998) -- 2.2.3.1 Mutational Analysis of Rat CD2 -- 2.2.3.2 What We Learnt -- 2.2.4 CD58 d1 (1999) -- 2.2.4.1 The Structure -- 2.2.4.2 What We Learnt -- 2.2.5 CD48 d1 (2006) -- 2.2.5.1 The Structure -- 2.2.5.2 What We Learnt -- 2.3 Cell-Cell Recognition and Costimulation: CD28 Family Proteins. , 2.3.1 sB7-1 (2000) -- 2.3.1.1 The Structure -- 2.3.1.2 What We Learnt -- 2.3.2 sCTLA-4/sB7-1 Complex (2001) -- 2.3.2.1 The Structure -- 2.3.2.2 What We Learnt -- 2.3.3 sCD28/5.11A1 Antibody Fab (2005) -- 2.3.3.1 The Structure -- 2.3.3.2 What We Learnt -- 2.3.4 sCTLA-4 (2011) -- 2.3.4.1 The Structure -- 2.3.4.2 What We Learnt -- 2.3.5 sPD-1 (2013) -- 2.3.5.1 The Structure and Interactions -- 2.3.5.2 What We Learnt -- 2.4 Concluding Remarks -- Acknowledgments -- References -- Chapter 3: Synthetic Antibody Engineering: Concepts and Applications -- 3.1 Introduction -- 3.2 Immunoglobulin Structure and Function -- 3.3 Engineering Phage-Displayed Antibody Libraries -- 3.4 Applications -- 3.4.1 Engineering of Conformation-Specific Antibodies -- 3.4.2 Engineering of Cross-Reactive Antibodies -- 3.4.3 Engineering of Antibodies Specific for Point-Mutants and PTMs -- 3.5 Conclusions -- References -- Chapter 4: Natural Killer Cell Receptors -- 4.1 Introduction -- 4.2 MHC-I Recognition by Ly49 Receptors -- 4.3 Ly49 Receptors Interact With MHC-I in Trans and Cis -- 4.4 Ly49A's Recognition of a Viral Immunoevasin -- 4.5 Recognition of MHC-I by KIR Receptors -- 4.6 Recognition of MHC-I by LILRs -- 4.7 LILR Recognition of the Viral Immunoevasin UL18 -- 4.8 Natural Cytotoxicity Receptors -- 4.9 Ligand Binding by NKG2D -- 4.10 HLA-E Recognition by NKG2/CD94 -- 4.11 Recognition of Cadherins by KLRG1 -- 4.12 C-type Lectin-like Receptor-Ligand Pairs in the NK Gene Complex -- 4.13 Perspective -- References -- Chapter 5: Structure-Function in Antibodies to Double-Stranded DNA -- 5.1 Anti-dsDNA Antibodies Are Pivotal in the Pathogenesis of Lupus Erythematosus -- 5.2 The Basic Features of Antigen Recognition by Anti-dsDNA Antibodies -- 5.3 The Constant Regions Contribute to Antigenic Specificity and Renal Pathogenicity of Anti-dsDNA Antibodies. , 5.4 The Structure of Anti-dsDNA Antibodies -- 5.5 Catalytic Properties of Anti-dsDNA Antibodies -- 5.6 DNA-Mimicking Peptides Bound by Anti-dsDNA Antibodies -- 5.7 Development of Novel Therapeutic Approaches Targeting Anti-dsDNA Antibodies In Vivo -- References -- Chapter 6: The Role of the Constant Region in Antibody-Antigen Interactions: Redefining the Modular Model of Immunoglobulin Structure -- 6.1 Introduction -- 6.2 Immunoglobulin Structure -- 6.3 The Modular Antibody Model -- 6.4 Evidence for Intramolecular Signaling Upon Antigen Binding -- 6.5 Constant Region Modulation of Antibody Properties -- 6.6 Concluding Remarks -- References -- Index -- Back Cover.