2fb4
From Proteopedia
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DIR PRIMAERSTRUKTUR DES KRISTALLISIERBAREN MONOKLONALEN IMMUNOGLOBULINS IGG1 KOL. II. AMINOSAEURESEQUENZ DER L-KETTE, LAMBDA-TYP, SUBGRUPPE I (GERMAN)
Overview
The immunoglobulin Kol was the first intact antibody molecule which was, characterized by high-resolution X-ray crystallography. Furthermore the, complete amino-acid sequence of the heavy (H)-chain is known. Here we, report the complete amino-acid sequence of the light (L)-chain of the, monoclonal immunoglobulin Kol (IgG1). The polypeptide has an Mr of 22,781, consists of 216 amino acids and due to its structure is of the, lambda-type. With the characteristic amino acids threonine, asparagine, threonine, glycine and lysine in positions 101, 114, 116, 154, and 165, respectively the Kol L-chain is of the Mcg isotype. With the proteins Mcg, Mot, Bur, Loc and Mem six myeloma-derived amino-acid sequences of the same, isotype are known. The amino-acid sequence of the N-terminal variable part, is characteristic of subgroup 1. This contribution completes the primary, structure of IgG1 Kol.
About this Structure
2FB4 is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1FB4. Full crystallographic information is available from OCA.
Reference
[The primary structure of crystallizable monoclonal immunoglobulin IgG1 Kol. II. Amino acid sequence of the L-chain, gamma-type, subgroup I], Kratzin HD, Palm W, Stangel M, Schmidt WE, Friedrich J, Hilschmann N, Biol Chem Hoppe Seyler. 1989 Mar;370(3):263-72. PMID:2713105
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