2RE9
Crystal structure of TL1A at 2.1 A
2RE9 の概要
エントリーDOI | 10.2210/pdb2re9/pdb |
分子名称 | TNF superfamily ligand TL1A, MAGNESIUM ION, GLYCEROL, ... (4 entities in total) |
機能のキーワード | vegi, homotrimer, metal binding, cytokine, membrane, transmembrane, hormone-growth factor complex, hormone/growth factor |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 61868.47 |
構造登録者 | Jin, T.C.,Guo, F.,Kim, S.,Howard, A.J.,Zhang, Y.Z. (登録日: 2007-09-25, 公開日: 2007-10-09, 最終更新日: 2023-08-30) |
主引用文献 | Jin, T.,Guo, F.,Kim, S.,Howard, A.,Zhang, Y.Z. X-ray crystal structure of TNF ligand family member TL1A at 2.1 A. Biochem.Biophys.Res.Commun., 364:1-6, 2007 Cited by PubMed Abstract: The TNF family has been one of the most intensively studied protein families in the past two decades and it has rapidly expanded through the era of genomics and bioinformatics. However, the structural basis of the functional and interactional similarities and differences of this family is poorly understood. TL1A is a recently identified TNF family member that has received increasing attention. Here, the crystal structure of human TL1A is reported. TL1A forms a homotrimer with each monomer assuming a jellyroll beta-sandwich fold. The CD loop in TL1A is the longest among the TNF ligand members with known structure and the AA' loop in TL1A is the second longest after that in TRAIL, where part of it is disordered. Both these loops are known to participate in receptor binding in TNFbeta/LTalpha. The AA' loop may be very different in other TL1A variants if the overall fold is to be preserved. PubMed: 17935696DOI: 10.1016/j.bbrc.2007.09.097 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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