2ig2
From Proteopedia
(New page: 200px<br /> <applet load="2ig2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ig2, resolution 3.0Å" /> '''DIR PRIMAERSTRUKTUR ...) |
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| - | [[Image:2ig2.gif|left|200px]]<br /> | + | [[Image:2ig2.gif|left|200px]]<br /><applet load="2ig2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2ig2" size=" | + | |
caption="2ig2, resolution 3.0Å" /> | caption="2ig2, resolution 3.0Å" /> | ||
'''DIR PRIMAERSTRUKTUR DES KRISTALLISIERBAREN MONOKLONALEN IMMUNOGLOBULINS IGG1 KOL. II. AMINOSAEURESEQUENZ DER L-KETTE, LAMBDA-TYP, SUBGRUPPE I (GERMAN)'''<br /> | '''DIR PRIMAERSTRUKTUR DES KRISTALLISIERBAREN MONOKLONALEN IMMUNOGLOBULINS IGG1 KOL. II. AMINOSAEURESEQUENZ DER L-KETTE, LAMBDA-TYP, SUBGRUPPE I (GERMAN)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The immunoglobulin Kol was the first intact antibody molecule which was | + | 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== | ==About this Structure== | ||
| - | 2IG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure | + | 2IG2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1IG2. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IG2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: immunoglobulin]] | [[Category: immunoglobulin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:52:24 2008'' |
Revision as of 15:52, 21 February 2008
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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
2IG2 is a Protein complex structure of sequences from Homo sapiens. This structure supersedes the now removed PDB entry 1IG2. 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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