NMR and structural genomics.
The role of NMR in structural genomics is outlined, with particular emphasis on using protein domains as targets. Strategies for domain expression, characterization, and labeling are presented.
Genomics↗
Biomedical subjects
David Staunton
Publications and source records attributed to David Staunton.
Mapping the heparin-binding site on the 13-14F3 fragment of fibronectin.
Fibronectin, a multifunctional glycoprotein of the extracellular matrix, plays a major role in cell adhesion. Various studies have revealed that the human 13th and 14th fibronectin type III domains (labeled (13)F3 and (14)F3 here) contain a heparin-binding site. Mapping of the heparin-binding sites of (13-14)F3, (13)F3, and (14)F3 by NMR chemical shift perturbation, isothermal titration calorimetry, and molecular modeling show that (13)F3 provides the dominant heparin-binding site and that the residues involved are within the first 29 amino acids of (13)F3. Predictions from earlier biochemical and modeling studies as well as the x-ray structure of (12-14)F3 were tested. It was shown that the positively charged residues that project into the solvent from the ABE face of the triple-stranded beta sheet on (13)F3 are involved in binding, but (14)F3 does not appear to contribute significantly to heparin binding.
Amino Acid Sequence↗