Comparative assessment of the ligand and metal ion binding properties of integrins alpha9beta1 and alpha4beta1.

@article{Pepinsky2002ComparativeAO,
  title={Comparative assessment of the ligand and metal ion binding properties of integrins alpha9beta1 and alpha4beta1.},
  author={Robert Blake Pepinsky and Richard A. Mumford and Ling Ling Chen and Diane R Leone and Suzanne E Amo and Gail Van Riper and Adrian Whitty and Brian M Dolinski and Roy R. Lobb and Dennis C Dean and Linda Li Chang and Conrad E Raab and Qian Si and William K. Hagmann and Russell B. Lingham},
  journal={Biochemistry},
  year={2002},
  volume={41 22},
  pages={7125-41}
}
Integrins alpha9beta1 and alpha4beta1 form a distinct structural class, but while alpha4beta1 has been subjected to extensive study, alpha9beta1 remains poorly characterized. We have used the small molecule N-(benzenesulfonyl)-(L)-prolyl-(L)-O-(1-pyrrolidinylcarbonyl)tyrosine (3) to investigate the biochemical properties of alpha9beta1 and directly compare these properties with those of alpha4beta1. Compound 3 has a high affinity for both integrins with K(D) values of < or =3 and 180 pM for… CONTINUE READING

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