1GK5

Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor

1GK5 の概要

• エントリーDOI: 10.2210/pdb1gk5/pdb
• NMR情報: BMRB: 5120
• 分子名称: Pro-epidermal growth factor,Protransforming growth factor alpha (1 entity in total)
• 機能のキーワード: growth factor, egf growth factor, chimeric
• 由来する生物種: Mus musculus (House Mouse); 詳細
• 細胞内の位置: Transforming growth factor alpha: Secreted, extracellular space. Protransforming growth factor alpha: Cell membrane; Single-pass type I membrane protein: P01135
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5257.78

構造登録者

Chamberlin, S.G.,Brennan, L.,Puddicombe, S.M.,Davies, D.E.,Turner, D.L. (登録日: 2001-08-08, 公開日: 2002-08-08, 最終更新日: 2024-11-13)

主引用文献

Chamberlin, S.,Brennan, L.,Puddicombe, S.,Davies, D.,Turner, D.
Solution Structure of the Megf/Tgfalpha44-50 Chimeric Growth Factor.
Eur.J.Biochem., 268:6247-, 2001

PubMed Abstract: The solution structure of the growth factor chimera mEGF/TGFalpha44-50 has been determined using an extended version of the dyana procedure for calculating structures from NMR data. The backbone fold and preferred orientation of the domains of the chimera are similar to those found in previous studies of EGF structures, and several H-bonds used as input constraints in those studies were found independently in the chimera. This shows that the modified activity of the chimera does not result from a major structural change. However, the improved precision of the structure presented here allows the origin of some unusual chemical shifts found in all of these compounds to be explained, as well as the results obtained from some site-specific mutants. Further studies of the properties of this chimeric growth factor should help to elucidate the mechanism(s) of hetero- and homodimerization of the c-erbB receptors.

PubMed: 11733021
DOI: 10.1046/J.0014-2956.2001.02581.X

実験手法

SOLUTION NMR