3HCT
Crystal structure of TRAF6 in complex with Ubc13 in the P1 space group
3HCT の概要
エントリーDOI | 10.2210/pdb3hct/pdb |
関連するPDBエントリー | 3HCS 3HCU |
分子名称 | TNF receptor-associated factor 6, Ubiquitin-conjugating enzyme E2 N, ZINC ION, ... (4 entities in total) |
機能のキーワード | cross-brace, beta-beta-alpha, coiled coil, cytoplasm, metal-binding, ubl conjugation, ubl conjugation pathway, zinc, zinc-finger, atp-binding, dna damage, dna repair, isopeptide bond, ligase, nucleotide-binding, signaling protein-ligase complex, signaling protein/ligase |
由来する生物種 | Homo sapiens (human) 詳細 |
細胞内の位置 | Cytoplasm : Q9Y4K3 Nucleus : P61088 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 31412.18 |
構造登録者 | Yin, Q.,Lin, S.-C.,Lamothe, B.,Lu, M.,Lo, Y.-C.,Hura, G.,Zheng, L.,Rich, R.L.,Campos, A.D.,Myszka, D.G.,Lenardo, M.J.,Darnay, B.G.,Wu, H. (登録日: 2009-05-06, 公開日: 2009-05-26, 最終更新日: 2023-09-06) |
主引用文献 | Yin, Q.,Lin, S.C.,Lamothe, B.,Lu, M.,Lo, Y.C.,Hura, G.,Zheng, L.,Rich, R.L.,Campos, A.D.,Myszka, D.G.,Lenardo, M.J.,Darnay, B.G.,Wu, H. E2 interaction and dimerization in the crystal structure of TRAF6. Nat.Struct.Mol.Biol., 16:658-666, 2009 Cited by PubMed Abstract: Tumor necrosis factor (TNF) receptor-associated factor (TRAF)-6 mediates Lys63-linked polyubiquitination for NF-kappaB activation via its N-terminal RING and zinc finger domains. Here we report the crystal structures of TRAF6 and its complex with the ubiquitin-conjugating enzyme (E2) Ubc13. The RING and zinc fingers of TRAF6 assume a rigid, elongated structure. Interaction of TRAF6 with Ubc13 involves direct contacts of the RING and the preceding residues, and the first zinc finger has a structural role. Unexpectedly, this region of TRAF6 is dimeric both in the crystal and in solution, different from the trimeric C-terminal TRAF domain. Structure-based mutagenesis reveals that TRAF6 dimerization is crucial for polyubiquitin synthesis and autoubiquitination. Fluorescence resonance energy transfer analysis shows that TRAF6 dimerization induces higher-order oligomerization of full-length TRAF6. The mismatch of dimeric and trimeric symmetry may provide a mode of infinite oligomerization that facilitates ligand-dependent signal transduction of many immune receptors. PubMed: 19465916DOI: 10.1038/nsmb.1605 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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