## Abstract A mass spectrometric protocol for identifying ligands with a wide range of affinities (3β101β Β΅M) and quantitative spectral analysis for nonβcovalent interactions have been developed using Src SH2 as a target. Dissociation constants of five compounds, three with a phospho moiety, one wit
Covalent binding of catechols to src family SH2 domains
β Scribed by Christopher T. Jagoe; Scott E. Kreifels; Jongming Li
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 192 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0960-894X
No coin nor oath required. For personal study only.
β¦ Synopsis
Src family SH2 domains contain an uncoupled cysteine residue, that, when arylated with air oxidized catechols, inhibits the protein from binding to otherwise high affinity peptide ligands. No inhibition is observed for Crk, Abl, or Grb2 SH2 domains.
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