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6XE6

Structure of Human Dispatched-1 (DISP1)

6XE6 の概要
エントリーDOI10.2210/pdb6xe6/pdb
EMDBエントリー22144
分子名称Protein dispatched homolog 1, CHOLESTEROL HEMISUCCINATE, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
機能のキーワードhedgehog, secretion, sterol binding, sterol-sensing domain, membrane protein
由来する生物種Homo sapiens (Human)
タンパク質・核酸の鎖数1
化学式量合計127153.59
構造登録者
Chen, H.,Liu, Y.,Li, X. (登録日: 2020-06-12, 公開日: 2020-07-08, 最終更新日: 2024-11-20)
主引用文献Chen, H.,Liu, Y.,Li, X.
Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis.
Life Sci Alliance, 3:-, 2020
Cited by
PubMed Abstract: Hedgehog (HH) signaling is essential for metazoan development. The HH ligand is secreted into the extracellular space by a cell surface protein named Dispatched-1 (DISP1). Here, we report the cryo-EM structure of human DISP1 protein. DISP1 contains 12 transmembrane helices (TMs) and two extracellular domains (ECDs). Its ECDs reveal an open state, in contrast to its structural homologues PTCH1 and NPC1, whose extracellular/luminal domains adopt a closed state. The low-resolution structure of the DISP1 complex with dual lipid-modified HH ligand reveals how the ECDs of DISP1 engage with HH ligand. Moreover, several cholesterol-like molecules are found in the TMs, implying a transport-like function of DISP1.
PubMed: 32646883
DOI: 10.26508/lsa.202000776
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (4.53 Å)
構造検証レポート
Validation report summary of 6xe6
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2026-02-04に公開中

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