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1E87

Human CD69 - trigonal form

1E87 の概要
エントリーDOI10.2210/pdb1e87/pdb
関連するPDBエントリー1E8I
分子名称EARLY ACTIVATION ANTIGEN CD69, ZINC ION, GLYCEROL, ... (4 entities in total)
機能のキーワードhematopoietic cell receptor, leucocyte, nkd, klr, sugar binding protein
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Membrane; Single-pass type II membrane protein: Q07108
タンパク質・核酸の鎖数1
化学式量合計13964.06
構造登録者
Tormo, J. (登録日: 2000-09-18, 公開日: 2000-09-26, 最終更新日: 2024-10-09)
主引用文献Llera, A.S.,Viedma, F.,Sanchez-Madrid, F.,Tormo, J.
Crystal Structure of the C-Type Lectin-Like Domain from the Human Hematopoietic Cell Receptor Cd69
J.Biol.Chem., 276:7312-, 2001
Cited by
PubMed Abstract: CD69, one of the earliest specific antigens acquired during lymphoid activation, acts as a signal-transducing receptor involved in cellular activation events, including proliferation and induction of specific genes. CD69 belongs to a family of receptors that modulate the immune response and whose genes are clustered in the natural killer (NK) gene complex. The extracellular portion of these receptors represent a subfamily of C-type lectin-like domains (CTLDs), which are divergent from true C-type lectins and are referred to as NK-cell domains (NKDs). We have determined the three-dimensional structure of human CD69 NKD in two different crystal forms. CD69 NKD adopts the canonical CTLD fold but lacks the features involved in Ca(2+) and carbohydrate binding by C-type lectins. CD69 NKD dimerizes noncovalently, both in solution and in crystalline state. The dimer interface consists of a hydrophobic, loosely packed core, surrounded by polar interactions, including an interdomain beta sheet. The intersubunit core shows certain structural plasticity that may facilitate conformational rearrangements for binding to ligands. The surface equivalent to the binding site of other members of the CTLD superfamily reveals a hydrophobic patch surrounded by conserved charged residues that probably constitutes the CD69 ligand-binding site.
PubMed: 11036086
DOI: 10.1074/JBC.M008573200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.5 Å)
構造検証レポート
Validation report summary of 1e87
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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