1HI7

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

Summary for 1HI7

• Entry DOI: 10.2210/pdb1hi7/pdb
• Related: 1PS2
• Descriptor: PS2 PROTEIN (1 entity in total)
• Functional Keywords: growth factor, cell motility, tumor suppressor, trefoil domain
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 13356.73

Authors

Williams, M.A.,Feeney, J. (deposition date: 2001-01-03, release date: 2001-01-03, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

SOLUTION NMR