2H3N
Crystal structure of a surrogate light chain (LAMBDA5 and VpreB) homodimer
2H3N の概要
| エントリーDOI | 10.2210/pdb2h3n/pdb |
| 関連するPDBエントリー | 2H32 |
| 分子名称 | VpreB protein, Ig lambda-5 (3 entities in total) |
| 機能のキーワード | beta sheets, v- and c-type immunoglobulin fold, immune system |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Secreted (Potential): P15814 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 48138.13 |
| 構造登録者 | |
| 主引用文献 | Bankovich, A.J.,Raunser, S.,Juo, Z.S.,Walz, T.,Davis, M.M.,Garcia, K.C. Structural insight into pre-B cell receptor function Science, 316:291-294, 2007 Cited by PubMed Abstract: The pre-B cell receptor (pre-BCR) serves as a checkpoint in B cell development. In the 2.7 angstrom structure of a human pre-BCR Fab-like fragment, consisting of an antibody heavy chain (HC) paired with the surrogate light chain, the "unique regions" of VpreB and lambda5 replace the complementarity-determining region 3 (CDR3) loop of an antibody light chain and appear to "probe" the HC CDR3, potentially influencing the selection of the antibody repertoire. Biochemical analysis indicates that the pre-BCR is impaired in its ability to recognize antigen, which, together with electron microscopic visualization of a pre-BCR dimer, suggests ligand-independent oligomerization as the likely signaling mechanism. PubMed: 17431183DOI: 10.1126/science.1139412 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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