2Z66
Crystal structure of the VT3 hybrid of human TLR4 and hagfish VLRB.61
2Z66 の概要
エントリーDOI | 10.2210/pdb2z66/pdb |
関連するPDBエントリー | 2Z62 2Z63 2Z64 2Z65 |
分子名称 | Variable lymphocyte receptor B, Toll-like receptor 4, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
機能のキーワード | tlr4, toll-like receptor, md-2, lps, leucine-rich repeat, glycoprotein, immune response, inflammatory response, innate immunity, membrane, transmembrane, immune system |
由来する生物種 | Eptatretus burgeri (inshore hagfish, human) 詳細 |
細胞内の位置 | Cell membrane ; Single- pass type I membrane protein : O00206 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 146512.37 |
構造登録者 | |
主引用文献 | Kim, H.M.,Park, B.S.,Kim, J.-I.,Kim, S.E.,Lee, J.,Oh, S.C.,Enkhbayar, P.,Matsushima, N.,Lee, H.,Yoo, O.J.,Lee, J.-O. Crystal Structure of the TLR4-MD-2 Complex with Bound Endotoxin Antagonist Eritoran Cell(Cambridge,Mass.), 130:906-917, 2007 Cited by PubMed Abstract: TLR4 and MD-2 form a heterodimer that recognizes LPS (lipopolysaccharide) from Gram-negative bacteria. Eritoran is an analog of LPS that antagonizes its activity by binding to the TLR4-MD-2 complex. We determined the structure of the full-length ectodomain of the mouse TLR4 and MD-2 complex. We also produced a series of hybrids of human TLR4 and hagfish VLR and determined their structures with and without bound MD-2 and Eritoran. TLR4 is an atypical member of the LRR family and is composed of N-terminal, central, and C-terminal domains. The beta sheet of the central domain shows unusually small radii and large twist angles. MD-2 binds to the concave surface of the N-terminal and central domains. The interaction with Eritoran is mediated by a hydrophobic internal pocket in MD-2. Based on structural analysis and mutagenesis experiments on MD-2 and TLR4, we propose a model of TLR4-MD-2 dimerization induced by LPS. PubMed: 17803912DOI: 10.1016/j.cell.2007.08.002 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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