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5M5V

Clathrin heavy chain N-terminal domain bound to a clathrin-box motif from hepatitis D virus large antigen (clade 2)

5M5V の概要
エントリーDOI10.2210/pdb5m5v/pdb
分子名称Clathrin heavy chain 1, Large delta antigen, GLYCEROL, ... (4 entities in total)
機能のキーワードendocytosis, hepatitis delta virus, hdag-l
由来する生物種Bos taurus (Bovine)
詳細
細胞内の位置Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P49951
タンパク質・核酸の鎖数8
化学式量合計87246.13
構造登録者
Muenzner, J.,Graham, S.C. (登録日: 2016-10-22, 公開日: 2016-11-23, 最終更新日: 2024-01-17)
主引用文献Muenzner, J.,Traub, L.M.,Kelly, B.T.,Graham, S.C.
Cellular and viral peptides bind multiple sites on the N-terminal domain of clathrin.
Traffic, 18:44-57, 2017
Cited by
PubMed Abstract: Short peptide motifs in unstructured regions of clathrin-adaptor proteins recruit clathrin to membranes to facilitate post-Golgi membrane transport. Three consensus clathrin-binding peptide sequences have been identified and structural studies show that each binds distinct sites on the clathrin heavy chain N-terminal domain (NTD). A fourth binding site for adaptors on NTD has been functionally identified but not structurally characterised. We have solved high resolution structures of NTD bound to peptide motifs from the cellular clathrin adaptors β2 adaptin and amphiphysin plus a putative viral clathrin adaptor, hepatitis D virus large antigen (HDAg-L). Surprisingly, with each peptide we observe simultaneous peptide binding at multiple sites on NTD and viral peptides binding to the same sites as cellular peptides. Peptides containing clathrin-box motifs (CBMs) with the consensus sequence LΦxΦ[DE] bind at the 'arrestin box' on NTD, between β-propeller blades 4 and 5, which had previously been thought to bind a distinct consensus sequence. Further, we structurally define the fourth peptide binding site on NTD, which we term the Royle box. In vitro binding assays show that clathrin is more readily captured by cellular CBMs than by HDAg-L, and site-directed mutagenesis confirms that multiple binding sites on NTD contribute to efficient capture by CBM peptides.
PubMed: 27813245
DOI: 10.1111/tra.12457
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.96 Å)
構造検証レポート
Validation report summary of 5m5v
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2026-04-15に公開中

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