Abstract
The novel phosphotyrosine (pTyr) mimetic 4'-carboxymethyloxy-3'-phosphonophenylalanine (Cpp) has been designed and incorporated into a series of nonpeptide inhibitors of the SH2 domain of pp60(c-Src) (Src) tyrosine kinase. A 2.2 A X-ray crystal structure of 1a bound to a mutant form of Lck SH2 domain provides insight regarding the structure-activity relationships and supports the design concept of this new pTyr mimetic.
MeSH terms
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Animals
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Benzamides / chemistry*
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Benzamides / pharmacology*
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Binding Sites
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Bone Resorption
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Crystallography, X-Ray
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Dentin / drug effects
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Drug Design
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / metabolism
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Enzyme Inhibitors / pharmacology*
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Magnetic Resonance Spectroscopy
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Molecular Mimicry
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Mutation
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Organophosphonates / chemistry*
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Organophosphonates / pharmacology*
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Osteoclasts / drug effects
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Osteoclasts / metabolism
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Phosphotyrosine / chemistry*
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Proto-Oncogene Proteins pp60(c-src) / antagonists & inhibitors*
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Proto-Oncogene Proteins pp60(c-src) / chemistry
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Proto-Oncogene Proteins pp60(c-src) / genetics
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Rabbits
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Structure-Activity Relationship
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src Homology Domains / drug effects*
Substances
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4-(2-acetamido-3-(1-(3-carbamoyl-4-(cyclohexylmethoxy)phenyl)ethylamino)-3-oxopropyl)-2-(carboxymethoxy)benzenephosphonic acid
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Benzamides
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Enzyme Inhibitors
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Organophosphonates
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Phosphotyrosine
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Proto-Oncogene Proteins pp60(c-src)