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1MJD

Structure of N-terminal domain of human doublecortin

1MJD の概要
エントリーDOI10.2210/pdb1mjd/pdb
関連するPDBエントリー1MFW 1MG4
NMR情報BMRB: 5482
分子名称DOUBLECORTIN (1 entity in total)
機能のキーワードdcx domain, ubiquitin-like fold, microtubule associated protein, signaling protein
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm: O43602
タンパク質・核酸の鎖数1
化学式量合計12972.49
構造登録者
主引用文献Kim, M.H.,Cierpicki, T.,Derewenda, U.,Krowarsch, D.,Feng, Y.,Devedjiev, Y.,Dauter, Z.,Walsh, C.A.,Otlewski, J.,Bushweller, J.H.,Derewenda, Z.S.
The DCX-domain Tandems of Doublecortin and Doublecortin-like Kinase
Nat.Struct.Biol., 10:324-333, 2003
Cited by
PubMed Abstract: The doublecortin-like domains (DCX), which typically occur in tandem, are novel microtubule-binding modules. DCX tandems are found in doublecortin, a 360-residue protein expressed in migrating neurons; the doublecortin-like kinase (DCLK); the product of the RP1 gene that is responsible for a form of inherited blindness; and several other proteins. Mutations in the gene encoding doublecortin cause lissencephaly in males and the 'double-cortex syndrome' in females. We here report a solution structure of the N-terminal DCX domain of human doublecortin and a 1.5 A resolution crystal structure of the equivalent domain from human DCLK. Both show a stable, ubiquitin-like tertiary fold with distinct structural similarities to GTPase-binding domains. We also show that the C-terminal DCX domains of both proteins are only partially folded. In functional assays, the N-terminal DCX domain of doublecortin binds only to assembled microtubules, whereas the C-terminal domain binds to both microtubules and unpolymerized tubulin.
PubMed: 12692530
DOI: 10.1038/nsb918
主引用文献が同じPDBエントリー
実験手法
SOLUTION NMR
構造検証レポート
Validation report summary of 1mjd
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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