1HI7: NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES

Citation:
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.
PDB ID: 1HI7Download
MMDB ID: 15515
PDB Deposition Date: 2001/1/3
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1HI7: dimeric; determined by author
Molecular Components in 1HI7
Label Count Molecule
Proteins (2 molecules)
2
PS2 Protein(Gene symbol: TFF1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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