3WBR
Crystal structure of carbohydrate recognition domain of Blood Dendritic Cell Antigen-2 (BDCA2) lectin (crystal form-3)
3WBR の概要
| エントリーDOI | 10.2210/pdb3wbr/pdb |
| 関連するPDBエントリー | 3WBP 3WBQ |
| 分子名称 | C-type lectin domain family 4 member C (2 entities in total) |
| 機能のキーワード | c-type lectin fold, immune receptor, complex-type n-glycan, carbohydrate binding protein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cell membrane ; Single-pass type II membrane protein : Q8WTT0 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 121022.97 |
| 構造登録者 | Nagae, M.,Ikeda, A.,Kitago, Y.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y. (登録日: 2013-05-20, 公開日: 2013-12-25, 最終更新日: 2024-11-13) |
| 主引用文献 | Nagae, M.,Ikeda, A.,Kitago, Y.,Matsumoto, N.,Yamamoto, K.,Yamaguchi, Y. Crystal structures of carbohydrate recognition domain of blood dendritic cell antigen-2 (BDCA2) reveal a common domain-swapped dimer. Proteins, 82:1512-1518, 2014 Cited by PubMed Abstract: We report on crystal structures of a carbohydrate recognition domain (CRD) of human C-type lectin receptor blood dendritic cell antigen-2 (BDCA2). Three different crystal forms were obtained at 1.8-2.3 Å resolution. In all three, the CRD has a basic C-type lectin fold, but a long loop extends away from the core domain to form a domain-swapped dimer. The structures of the dimers from the three different crystal forms superimpose well, indicating that domain swapping and dimer formation are energetically stable. The structure of the dimer is compared with other domain-swapped proteins, and a possible regulation mechanism of BDCA2 is discussed. PubMed: 24425442DOI: 10.1002/prot.24504 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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