1JWU
Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the superantigen SEC3 Variant 3B2
1JWU の概要
| エントリーDOI | 10.2210/pdb1jwu/pdb |
| 関連するPDBエントリー | 1JWM 1JWS |
| 分子名称 | HLA class II histocompatibility antigen, DR alpha chain, HLA class II histocompatibility antigen, DR-1 beta chain, HA peptide, ... (5 entities in total) |
| 機能のキーワード | hla-dr1 alpha subunit, hla-dr1 beta subunit, mutation, immune system |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cell membrane; Single-pass type I membrane protein: P01903 P04229 Secreted: P0A0L5 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 72464.44 |
| 構造登録者 | Sundberg, E.J.,Andersen, P.S.,Schlievert, P.M.,Karjalainen, K.,Mariuzza, R.A. (登録日: 2001-09-05, 公開日: 2003-07-08, 最終更新日: 2024-11-06) |
| 主引用文献 | Sundberg, E.J.,Andersen, P.S.,Schlievert, P.M.,Karjalainen, K.,Mariuzza, R.A. Structural, energetic, and functional analysis of a protein-protein interface at distinct stages of affinity maturation Structure, 11:1151-1161, 2003 Cited by PubMed Abstract: Due to a paucity of studies that synthesize structural, energetic, and functional analyses of a series of protein complexes representing distinct stages in an affinity maturation pathway, the biophysical basis for the molecular evolution of protein-protein interactions is poorly understood. Here, we combine crystal structures and binding-free energies of a series of variant superantigen (SAG)-major histocompatibility complex (MHC) class II complexes exhibiting increasingly higher affinity to reveal that this affinity maturation pathway is controlled largely by two biophysical factors: shape complementarity and buried hydrophobic surface. These factors, however, do not contribute equivalently to the affinity maturation of the interface, as the former dominates the early steps of the maturation process while the latter is responsible for improved binding in later steps. Functional assays reveal how affinity maturation of the SAG-MHC interface corresponds to T cell activation by SAGs. PubMed: 12962633DOI: 10.1016/S0969-2126(03)00187-4 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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