3IKC
Structure of S67-27 in Complex with Kdo(2.8)-7-O-methyl-Kdo
3IKC の概要
エントリーDOI | 10.2210/pdb3ikc/pdb |
関連するPDBエントリー | 3IJH 3IJS 3IJY |
分子名称 | Immunoglobulin light chain (IGG3), Immunoglobulin heavy chain (IGG3), 3-deoxy-alpha-D-manno-oct-2-ulopyranosonic acid-(2-8)-(1E)-prop-1-en-1-yl 3-deoxy-7-O-methyl-alpha-D-manno-oct-2-ulopyranosidonic acid, ... (5 entities in total) |
機能のキーワード | antibody, kdo, chlamydia, lps, fab, carbohydrate, immune system |
由来する生物種 | Mus musculus (mouse) 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 98316.17 |
構造登録者 | |
主引用文献 | Brooks, C.L.,Blackler, R.J.,Sixta, G.,Kosma, P.,Muller-Loennies, S.,Brade, L.,Hirama, T.,Mackenzie, C.R.,Brade, H.,Evans, S.V. The role of CDR H3 in antibody recognition of a synthetic analog of a lipopolysaccharide antigen. Glycobiology, 20:138-147, 2010 Cited by PubMed Abstract: In order to explore the structural basis for adaptability in near germline monoclonal antibodies (mAb), we have examined the specificity of the promiscuous mAb S67-27 to both naturally derived carbohydrate antigens and a variety of synthetic nonnatural antigens based on the bacterial lipopolysaccharide component 3-deoxy-alpha-D-manno-oct-2-ulosonic acid (Kdo). One such analog, a 7-O-methyl (7-O-Me) Kdo disaccharide, was found to bind to the antibody with at least 30-fold higher affinity than any other antigen tested. The structure of S67-27 in complex with this analog and three other naturally occurring Kdo antigens revealed that the enhanced affinity of the mAb for the synthetic analog was accomplished by the strategic positioning of CDR H3 away from a conserved Kdo binding pocket that allowed the formation of new antibody-antigen contacts. Furthermore, the comparison of this structure with the structures of related mAbs revealed how the position and structure of CDR H3 influence the specificity or promiscuity of near-germline carbohydrate-recognizing antibodies by altering the architecture of the combining site. PubMed: 19767317DOI: 10.1093/glycob/cwp150 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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