1.
J Med Chem
; 44(26): 4737-40, 2001 Dec 20.
Article
in English
| MEDLINE
| ID: mdl-11741491
ABSTRACT
Structure-based in-silico screening was carried out for the Syk C-terminal SH2 domain. Fragments that could interact with the pY or pY+1 pockets were selected by our in-silico screening. After tethering two fragments bound to these pockets, we have designed and synthesized new compounds that show favorable interaction with the pY+3 pocket. One such compound, having a cyclohexylmalonic acid moiety identified as a novel potent phosphotyrosyl mimetic, exhibited an affinity comparable to that of the monophosphorylated ligand peptide.
Subject(s)
Cyclohexanes/chemical synthesis , Enzyme Precursors/antagonists & inhibitors , Malonates/chemical synthesis , Protein-Tyrosine Kinases/antagonists & inhibitors , src Homology Domains , Binding, Competitive , Cyclohexanes/chemistry , Intracellular Signaling Peptides and Proteins , Ligands , Magnetic Resonance Spectroscopy , Malonates/chemistry , Models, Molecular , Molecular Mimicry , Phosphotyrosine/chemistry , Protein Structure, Tertiary , Syk Kinase
2.
J Antibiot (Tokyo)
; 54(1): 109-12, 2001 Jan.
Article
in English
| MEDLINE
| ID: mdl-11269709
3.
J Antibiot (Tokyo)
; 53(10): 1231-4, 2000 Oct.
Article
in English
| MEDLINE
| ID: mdl-11132974