BIOMAT Database Logo BIOMAT Database Logo

Structure-function relationships of immunoglobulin G. 1980

R H Painter, and K J Dorrington

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D007143 Immunoglobulin Heavy Chains The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa. Immunoglobulins, Heavy-Chain,Heavy-Chain Immunoglobulins,Ig Heavy Chains,Immunoglobulin Heavy Chain,Immunoglobulin Heavy Chain Subgroup VH-I,Immunoglobulin Heavy Chain Subgroup VH-III,Heavy Chain Immunoglobulins,Heavy Chain, Immunoglobulin,Heavy Chains, Ig,Heavy Chains, Immunoglobulin,Immunoglobulin Heavy Chain Subgroup VH I,Immunoglobulin Heavy Chain Subgroup VH III,Immunoglobulins, Heavy Chain
D007147 Immunoglobulin Light Chains Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule. Ig Light Chains,Immunoglobulins, Light-Chain,Immunoglobulin Light Chain,Immunoglobulin Light-Chain,Light-Chain Immunoglobulins,Chains, Ig Light,Chains, Immunoglobulin Light,Immunoglobulins, Light Chain,Light Chain Immunoglobulins,Light Chain, Immunoglobulin,Light Chains, Ig,Light Chains, Immunoglobulin,Light-Chain, Immunoglobulin
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D011961 Receptors, Fc Molecules found on the surface of some, but not all, B-lymphocytes, T-lymphocytes, and macrophages, which recognize and combine with the Fc (crystallizable) portion of immunoglobulin molecules. Fc Receptors,Fc Receptor,Receptor, Fc
D002621 Chemistry A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
D003172 Complement C1 The first complement component to act in the activation of CLASSICAL COMPLEMENT PATHWAY. It is a calcium-dependent trimolecular complex made up of three subcomponents: COMPLEMENT C1Q; COMPLEMENT C1R; and COMPLEMENT C1S at 1:2:2 ratios. When the intact C1 binds to at least two antibodies (involving C1q), C1r and C1s are sequentially activated, leading to subsequent steps in the cascade of COMPLEMENT ACTIVATION. C1 Complement,Complement 1,Complement Component 1,C1, Complement,Complement, C1,Component 1, Complement
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining

Related Publications

R H Painter, and K J Dorrington
Structure-function relationships in human immunoglobulin E.
January 1978, Immunological reviews,
R H Painter, and K J Dorrington
[Structure and function of immunoglobulin G (author's transl)].
September 1974, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
R H Painter, and K J Dorrington
Correspondence between structure and function of immunoglobulin G subclasses.
January 1981, Haematologia,
R H Painter, and K J Dorrington
[Human immunoglobulin G carbohydrate chain--its structure, function, and abnormality].
April 1994, Ryumachi. [Rheumatism],
R H Painter, and K J Dorrington
Structure/function relationships of axon-associated adhesion receptors of the immunoglobulin superfamily.
October 1996, Current opinion in neurobiology,
R H Painter, and K J Dorrington
Structure-function relationships of the G domain, a canonical switch motif.
January 2011, Annual review of biochemistry,
R H Painter, and K J Dorrington
Structure and Dynamics of Immunoglobulin G Glycoproteins.
January 2018, Advances in experimental medicine and biology,
R H Painter, and K J Dorrington
Immunoglobulin structure and function.
January 1969, Advances in internal medicine,
R H Painter, and K J Dorrington
Immunoglobulin structure and function.
January 1988, Current opinion in immunology,
R H Painter, and K J Dorrington
Immunoglobulin: structure and function.
January 1979, Cutis,
Copied contents to your clipboard!