1HI7

NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES

1HI7 の概要

• エントリーDOI: 10.2210/pdb1hi7/pdb
• 関連するPDBエントリー: 1PS2
• 分子名称: PS2 PROTEIN (1 entity in total)
• 機能のキーワード: growth factor, cell motility, tumor suppressor, trefoil domain
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13356.73

構造登録者

Williams, M.A.,Feeney, J. (登録日: 2001-01-03, 公開日: 2001-01-03, 最終更新日: 2024-10-09)

主引用文献

Williams, M.A.,Westley, B.R.,May, F.E.,Feeney, J.
The Solution Structure of the Disulphide-Linked Dimeric of the Human Trefoil Protein Tff1
FEBS Lett., 493:70-, 2001

PubMed Abstract: The trefoil factor family protein, TFF1, forms a homodimer, via a disulphide linkage, that has greater activity in wound healing assays than the monomer. Having previously determined a high-resolution solution structure of a monomeric analogue of TFF1, we now investigate the structure of the homodimer formed by the native sequence. The two putative receptor/ligand recognition domains are found to be well separated, at opposite ends of a flexible linker. This contrasts sharply with the known fixed and compact arrangement of the two trefoil domains of the closely related TFF2, and has significant implications for the mechanism of action and functional specificity of the TFF of proteins.

PubMed: 11286998
DOI: 10.1016/S0014-5793(01)02276-1

実験手法

SOLUTION NMR