2J5H

NMR analysis of mouse CRIPTO CFC domain

2J5H の概要

• エントリーDOI: 10.2210/pdb2j5h/pdb
• NMR情報: BMRB: 7299
• 分子名称: TERATOCARCINOMA-DERIVED GROWTH FACTOR (1 entity in total)
• 機能のキーワード: hormone/growth factor, growth factor, egf-cfc family, cripto, tumour progression, cysteine-rich domains, hormone-growth factor complex
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 4466.31

構造登録者

Calvanese, L.,Saporito, A.,Marasco, D.,D'Auria, G.,Minchiotti, G.,Pedone, C.,Paolillo, L.,Falcigno, L.,Ruvo, M. (登録日: 2006-09-18, 公開日: 2006-10-02, 最終更新日: 2024-10-16)

主引用文献

Calvanese, L.,Saporito, A.,Marasco, D.,D'Auria, G.,Minchiotti, G.,Pedone, C.,Paolillo, L.,Falcigno, L.,Ruvo, M.
Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala.
J. Med. Chem., 49:7054-7062, 2006

PubMed Abstract: We report here for the first time the solution structures at pH 3 and pH 6 of the synthetic CFC domain of mouse Cripto and of the point mutated variant W107A that is unable to bind to the Alk4 Cripto receptor. NMR data confirm that the CFC domain has a C1-C4, C2-C6, C3-C5 disulfide pattern and show that structures are rather flexible and globally extended, with three noncanonical antiparallel strands. His104 and Trp107 side chains protrude from a protein edge and are strongly exposed to solvent, supporting previous evidence of direct involvement in receptor binding. On the opposite molecule side, several nonpolar residues are gathered, forming a large hydrophobic patch that supposedly acts as interface with the cell membrane or the adjacent EGF-like domain. A second hydrophilic patch surrounding His104 and Trp107 is present only in the wild type variant, suggesting a possible involvement in modulating Alk4 recognition.

PubMed: 17125258
DOI: 10.1021/jm060772r

実験手法

SOLUTION NMR