A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Small molecule designed to target metal binding site in the alpha 2I domain inhibits integrin function
Tekijät: Kapyla J, Pentikainen OT, Nyronen T, Nissinen L, Lassander S, Jokinen J, Lahti M, Marjamaki A, Johnson MS, Heino J,
Kustantaja: AMER CHEMICAL SOC
Julkaisuvuosi: 2007
Journal: Journal of Medicinal Chemistry
Tietokannassa oleva lehden nimi: JOURNAL OF MEDICINAL CHEMISTRY
Lehden akronyymi: J MED CHEM
Vuosikerta: 50
Numero: 11
Aloitussivu: 2742
Lopetussivu: 2746
Sivujen määrä: 5
ISSN: 0022-2623
DOI: https://doi.org/10.1021/jm070063t
Verkko-osoite: http://pubs.acs.org/doi/abs/10.1021/jm070063t
Tiivistelmä
Integrin alpha 2 beta 1 is a potential target molecule in drug development. We have established "design" criteria for molecules that bind to the "closed" conformation of alpha 2I domain via Mg2+ in MIDAS (metal ion dependent adhesion site) while simultaneously forming interactions with neighboring amino acid residues. Specific tetracyclic Streptomyces products belonging to the group of aromatic polyketides fulfill our criteria and inhibit alpha 2 beta 1 integrin. All previously described inhibitors of alpha I domain integrins act in an allosteric manner.
Integrin alpha 2 beta 1 is a potential target molecule in drug development. We have established "design" criteria for molecules that bind to the "closed" conformation of alpha 2I domain via Mg2+ in MIDAS (metal ion dependent adhesion site) while simultaneously forming interactions with neighboring amino acid residues. Specific tetracyclic Streptomyces products belonging to the group of aromatic polyketides fulfill our criteria and inhibit alpha 2 beta 1 integrin. All previously described inhibitors of alpha I domain integrins act in an allosteric manner.
Research Areas
1/2
Turun yliopiston Tutkimustietojärjestelmän portaali