Title : Exploring the binding conformations of bulkier dipeptide amide inhibitors in constitutive nitric oxide synthases.

Pub. Date : 2005 Nov 22

PMID : 16285725






5 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 A series of L-nitroarginine-based dipeptide inhibitors are highly selective for neuronal nitric oxide synthase (nNOS) over the endothelial isoform (eNOS). Dipeptides nitric oxide synthase 1 Homo sapiens
2 A series of L-nitroarginine-based dipeptide inhibitors are highly selective for neuronal nitric oxide synthase (nNOS) over the endothelial isoform (eNOS). Dipeptides nitric oxide synthase 1 Homo sapiens
3 Crystal structures of these dipeptides bound to both isoforms revealed two different conformations, curled in nNOS and extended in eNOS, corresponding to higher and lower binding affinity to the two isoforms, respectively. Dipeptides nitric oxide synthase 1 Homo sapiens
4 Another residue farther away from the active site, Met336 in nNOS (Val106 in eNOS), is in contact with bulkier dipeptide inhibitors. Dipeptides nitric oxide synthase 1 Homo sapiens
5 Here we report crystal structures and inhibition constants for bulkier dipeptide inhibitors bound to nNOS and eNOS that illustrate the important role played by residues near the entry to the active site in isoform selective inhibition. Dipeptides nitric oxide synthase 1 Homo sapiens