2J5H: NMR analysis of mouse CRIPTO CFC domain

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.
PDB ID: 2J5HDownload
MMDB ID: 74717
PDB Deposition Date: 2006/9/18
Updated in MMDB: 2009/07
Experimental Method:
solution nmr
Similar Structures:
Biological Unit for 2J5H: monomeric; determined by author
Molecular Components in 2J5H
Label Count Molecule
Protein (1 molecule)
Teratocarcinoma-derived Growth Factor(Gene symbol: Tdgf1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB