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5FWT

Wnt modulator Kremen crystal form I at 2.10A

5FWT の概要
エントリーDOI10.2210/pdb5fwt/pdb
関連するPDBエントリー5FWS 5FWU 5FWV 5FWW
分子名称KREMEN PROTEIN 1, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
機能のキーワードsignaling protein, wnt, cell surface, signalling, membrane protein
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Membrane ; Single-pass type I membrane protein : Q96MU8
タンパク質・核酸の鎖数1
化学式量合計45350.45
構造登録者
Zebisch, M.,Jackson, V.A.,Jones, E.Y. (登録日: 2016-02-21, 公開日: 2016-07-20, 最終更新日: 2024-10-09)
主引用文献Zebisch, M.,Jackson, V.A.,Zhao, Y.,Jones, E.Y.
Structure of the Dual-Mode Wnt Regulator Kremen1 and Insight Into Ternary Complex Formation with Lrp6 and Dickkopf
Structure, 24:1599-, 2016
Cited by
PubMed Abstract: Kremen 1 and 2 have been identified as co-receptors for Dickkopf (Dkk) proteins, hallmark secreted antagonists of canonical Wnt signaling. We present here three crystal structures of the ectodomain of human Kremen1 (KRM1ECD) at resolutions between 1.9 and 3.2 Å. KRM1ECD emerges as a rigid molecule with tight interactions stabilizing a triangular arrangement of its Kringle, WSC, and CUB structural domains. The structures reveal an unpredicted homology of the WSC domain to hepatocyte growth factor. We further report the general architecture of the ternary complex formed by the Wnt co-receptor Lrp5/6, Dkk, and Krm, determined from a low-resolution complex crystal structure between β-propeller/EGF repeats (PE) 3 and 4 of the Wnt co-receptor LRP6 (LRP6PE3PE4), the cysteine-rich domain 2 (CRD2) of DKK1, and KRM1ECD. DKK1CRD2 is sandwiched between LRP6PE3 and KRM1Kringle-WSC. Modeling studies supported by surface plasmon resonance suggest a direct interaction site between Krm1CUB and Lrp6PE2.
PubMed: 27524201
DOI: 10.1016/J.STR.2016.06.020
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.1 Å)
構造検証レポート
Validation report summary of 5fwt
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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