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1C9L

PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN

1C9L の概要
エントリーDOI10.2210/pdb1c9l/pdb
関連するPDBエントリー1C9I
分子名称CLATHRIN, B-ADAPTIN 3 (2 entities in total)
機能のキーワードbeta-propeller, helical hairpin, endocytosis-exocytosis complex, endocytosis/exocytosis
由来する生物種Rattus norvegicus (Norway rat)
詳細
細胞内の位置Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P11442
タンパク質・核酸の鎖数4
化学式量合計81463.26
構造登録者
ter Haar, E.,Harrison, S.C.,Kirchhausen, T. (登録日: 1999-08-02, 公開日: 2000-02-07, 最終更新日: 2024-02-07)
主引用文献ter Haar, E.,Harrison, S.C.,Kirchhausen, T.
Peptide-in-groove interactions link target proteins to the beta-propeller of clathrin.
Proc.Natl.Acad.Sci.USA, 97:1096-1100, 2000
Cited by
PubMed Abstract: The "WD40" domain is a widespread recognition module for linking partner proteins in intracellular networks of signaling and sorting. The clathrin amino-terminal domain, which directs incorporation of cargo into coated pits, is a beta-propeller closely related in structure to WD40 modules. The crystallographically determined structures of complexes of the clathrin-terminal domain with peptides derived from two different cargo adaptors, beta-arrestin 2 and the beta-subunit of the AP-3 complex, reveal strikingly similar peptide-in-groove interactions. The two peptides in our structures contain related, five-residue motifs, which form the core of their contact with clathrin. A number of other proteins involved in endocytosis have similar "clathrin-box" motifs, and it therefore is likely that they all bind the terminal domain in the same way. We propose that a peptide-in-groove interaction is an important general mode by which beta-propellers recognize specific target proteins.
PubMed: 10655490
DOI: 10.1073/pnas.97.3.1096
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.9 Å)
構造検証レポート
Validation report summary of 1c9l
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2024-10-30に公開中

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