5N4J
human Fab fragment 10C3 against NHBA from Neisseria meningitidis
5N4J の概要
エントリーDOI | 10.2210/pdb5n4j/pdb |
分子名称 | LIGHT CHAIN, HEAVY CHAIN (3 entities in total) |
機能のキーワード | fab fragment, antibody, human, immune system |
由来する生物種 | Homo sapiens (Human) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 50085.38 |
構造登録者 | |
主引用文献 | Maritan, M.,Cozzi, R.,Lo Surdo, P.,Veggi, D.,Bottomley, M.J.,Malito, E. Crystal structures of human Fabs targeting the Bexsero meningococcal vaccine antigen NHBA. Acta Crystallogr F Struct Biol Commun, 73:305-314, 2017 Cited by PubMed Abstract: Neisserial heparin-binding antigen (NHBA) is a surface-exposed lipoprotein from Neisseria meningitidis and is a component of the meningococcus B vaccine Bexsero. As part of a study to characterize the three-dimensional structure of NHBA and the molecular basis of the human immune response to Bexsero, the crystal structures of two fragment antigen-binding domains (Fabs) isolated from human monoclonal antibodies targeting NHBA were determined. Through a high-resolution analysis of the organization and the amino-acid composition of the CDRs, these structures provide broad insights into the NHBA epitopes recognized by the human immune system. As expected, these Fabs also show remarkable structural conservation, as shown by a structural comparison of 15 structures of apo Fab 10C3 which were obtained from crystals grown in different crystallization conditions and were solved while searching for a complex with a bound NHBA fragment or epitope peptide. This study also provides indirect evidence for the intrinsically disordered nature of two N-terminal regions of NHBA. PubMed: 28580917DOI: 10.1107/S2053230X17006021 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.503 Å) |
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