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Structural and functional dynamics of the hinge region of IgG

Siobhan A. Hindley

Structural and functional dynamics of the hinge region of IgG

by Siobhan A. Hindley

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Published by University of Birmingham in Birmingham .
Written in English


Edition Notes

Thesis (Ph.D) - University of Birmingham, Department of Immunology, Faculty of Medicine and Dentistry.

Statementby Siobhan A. Hindley.
ID Numbers
Open LibraryOL22319196M

The book provides an exhaustive coverage of important topics such as temperature stresses. elastic constants, bending moments, shear forces, theory of simple bending, analysis and design of shafts, stepped, indeterminate and compound shafts, close- and open-coiled helical springs, Euler equations and Rankine formula for columns, and Mohr's circle. INTRODUCTION. Cell shape and movement form the basis for several biological phenomena such as morphogenesis, invasion, and metastasis. The actin cytoskeleton is a major determinant of changes in cell shape, and interactions between actin filaments and the cell membrane are essential for cell adhesion, spreading, and migration, as well as for signal transduction (Hall, ; Schoenwaelder and.

Flexing of the DI-DII hinge region is thought to be important for exposing the fusion loop of the virus E protein at low pH so as to facilitate the fusion of virus to the endosomal membrane (Bressanelli et al, ; Modis et al, ). HMAb 1F4, which binds to this region, may prevent the structural changes required for fusion. Functional analyses demonstrated that the KA and L50A mutantsmore» Structural comparisons indicated that the 'reconstituted' MAM monomer from the domain-swapped dimer displays large differences at the hinge regions from the MAM{sub wt} molecule in the receptor-bound form.

Get set. Go! The excited‐state hydrogen atom transfer of a phenol‐(ammonia) 5 hexamer is like a race. In their Communication on page ff. C. Jouvet, M. Fujii et al. show by time‐resolved spectroscopy that an electron jumps like a hare, reaching the solvent “princess” within 3 picoseconds of photoexcitation and leaving its partner, a proton, behind. Discuss; Classifications. C — CHEMISTRY; METALLURGY; C07 — ORGANIC CHEMISTRY; C07K — PEPTIDES; C07K16/00 — Immunoglobulins [IGs], e.g. monoclonal or Cited by:


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Structural and functional dynamics of the hinge region of IgG by Siobhan A. Hindley Download PDF EPUB FB2

It is also important to note that much of the limited literature on the functional characterization of structural dynamics and antibody stability of varying immunoglobulin isoforms comes from mutagenesis studies that have examined the effects of selective mutations of specific hinge-region residues through observation of the subsequent changes Cited by: 8.

The crystal structure of IgG 1 b12 MAb was the first IgG for which the entire structure, including the hinge, was intact and ordered (Saphire et al., ).While an IgG antibody is constructed of a seemingly symmetrical H 2 L 2 structure, the analysis of b12 demonstrated that the crystal structure of the antibody showed asymmetry of structure, in part due to crystal packing and in part, due to.

IgG3 represents approximately 8% of the total amount of IgG in human serum and stands out from the other IgG subclasses because of its elongated hinge region and enhanced effector functions. The functional properties of the four IgG subclasses partly result from the sequence differences of their hinge regions as some amino acids of the lower hinge region are located within or in the.

Antibody molecules have a highly specialized structure that can mediate biological response upon specifically binding to an antigen. This chapter introduces readers to the chemical structure of antibodies, with specific focus on the structure of immunoglobulin G (IgG).Cited by: 3.

Engineering of fragment crystallizable (Fc) domains of therapeutic immunoglobulin (IgG) antibodies to eliminate their immune effector functions while retaining other Fc characteristics has numerous applications, including blocking antigens on Fc gamma (Fcγ) receptor-expressing immune cells.

We previously reported on a human IgG2 variant termed IgG2σ with barely detectable activity in Cited by: 6. In mammals, antibodies exist in five major classes or isotypes possessing distinct structures and functions ().The five main antibody isotypes (IgG, IgM, IgA, IgE, and IgD) are determined by five different C H types (gamma γ, mu μ, alpha α, epsilon ε, and delta δ, respectively).

The various C H classes differ in size and structure, with γ, α, and δ consisting of three discrete domains Cited by: 1. An antibody (Ab), also known as an immunoglobulin (Ig), is a large, Y-shaped protein produced mainly by plasma cells that is used by the immune system to neutralize pathogens such as pathogenic bacteria and antibody recognizes a unique molecule of the pathogen, called an antigen, via the fragment antigen-binding (Fab) variable region.

Each tip of the "Y" of an antibody contains a. a | Immunoglobulin G (IgG) has two heavy and two light chains, and its crystallizable fragment (Fc) region can bind to Fcγ receptors and some proteins of the complement system.

The IgG Fc region contains two N -glycans, one per heavy chain, attached at Asn; these glycans contribute to the structural integrity of the Fc region and to its Cited by: An allosteric mechanism for the generation of long‐distance structural alterations in Fab fragments of antibodies in immune complexes has been postulated and tested in theoretical and experimental Cited by: The detection and characterization of unexpected disulfide-mediated structural variants of human immunoglobulin G2 (IgG2) antibodies was recently the subject of two copublications.(1, 2) In this paper, we present data to confirm the previously reported structures and elucidate the complete disulfide connectivity of each variant through the application of a novel analytical by:   Abstract.

Immunoglobulin G (IgG) is a major serum glycoprotein that exerts the role of antibody in the immune system. This multifunctional glycoprotein couples antigen recognition with a variety of effector functions promoted via interactions with various IgG-binding proteins.

Given its versatile functionality, IgG has recently been used for therapeutic : Hirokazu Yagi, Saeko Yanaka, Koichi Kato. Ig glycosylation is conserved at particular glycosites in the constant region of the Ig heavy chain.

In IgG, N-glycosylation is conserved at Asn (Recio et al. ) of the Fc region (Takimori et al. ).In fact, the constant regions of the Fc stem interact via their attached glycan chains (Deisenhofer ).Takimori et al.

() investigated IgG glycosylation over lactation and Cited by: These functional data were in line with those obtained analysing CD62P expression. Moreover, miRp transfection was associated with the down-regulation of a disintegrin and metalloproteinase-9 (ADAM9) messenger RNA (mRNA), a validated target of miRp, and of Plexin B2 (PLXNB2) mRNA and protein, an actin dynamics regulator.

(A) Structural characteristics of type I and type II FcγRs. Type I FcγRs belong to the Ig receptor superfamily and are composed of two or three extracellular Ig-like domains that interact with the IgG Fc domain at the hinge-proximal region of the C H 2 domain.

Type II FcγRs comprise DC-SIGN and CD23, both C-type lectin receptors, which bind Cited by:   The interactions appear highly discontinuous in nature, as HM14c10 binds to all three domains of the E protein of DENV The majority of the HM14cE1 interactions are formed through the heavy chains of both antibodies.

The V H region of HM14c10 interacts mainly with domain I, while its V L region binds at the hinge region connecting domains Cited by: 3. The red blood cell membrane (RBCM) is constructed primarily of an anastomosing spectrin-actin protein skeleton connected at regular intervals to the integral membrane proteins, band 3 and glycophorin C, via the bridging proteins, ankyrin, and protein Because the membrane is easily isolated, architecturally simple, and compositionally related to many other membranes, it is commonly Cited by: Human immunoglobulin G (IgG) is a protein of kDa that consists of two heavy (H) and two light (L) chains interlinked via a flexible hinge region.

The complete molecule consists of the Fab and the Fc regions (Figure 4A). Antigens are bound to the Fab region of IgG, which is formed by a piece of the H chain linked to the full L by: 7.

Dynamics of the interaction of human IgG subtype immune complexes with cells expressing R and H allelic forms of a low-affinity Fc gamma receptor CD32A.

J Immunol– Crossref, Medline, Google Scholar; Sondermann P, Huber R, Oosthuizen V, Jacob U (). The A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII by: 6. Recent advances in human genomics, gene regulation, structural biology, cell signaling, and immunobiology have greatly enhanced our understanding of this important class of antibody.

This book is designed to serve as a concise reference of the present knowledge of the biology of IgA, including structure of IgA and its interaction with Fc.

download IMMUNOLOGY A Short Course 7th Edition Pdf for free. 51 Hinge Region, 51 Variable Region, 51 Immunoglobulin Variants, 53 Isotypes, 53 Allotypes, 54 Idiotypes, 54 Structural Features of. Cluster of differentiation 20 (CD20) is a membrane protein that defines most B cell populations and is the target of therapeutic antibodies to treat malignancies and autoimmune disorders.

Rougé et al. present the structure of CD20 bound to the antibody rituximab that activates the complement system to kill B cells. CD20 forms a dimer and each monomer binds one rituximab antigen-binding Cited by: 1.(C) Model of the IgG/FcRn/SA ternary complex is presented.

The model was built from the HSA13/hFcRn structure, the rat Fc/rFcRn structure (PDB code 1FRT), and a full human IgG1 (1HZH). The IgG heavy chain is dark orange, and the light chain is light orange. The Fc portion of IgG occupies the diametrically opposite side of FcRn from by: