Title : The flexibility of P-glycoprotein for its poly-specific drug binding from molecular dynamics simulations.

Pub. Date : 2013

PMID : 22888853






1 Functional Relationships(s)
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1 Particularly, the flexibility of the side chains of aromatic residues (Phe and Tyr) allows them to form rotamers with different orientations in the binding pocket, which plays a critical role for the poly-specificity of the drug-binding cavity of P-gp. Tyrosine ATP binding cassette subfamily B member 1 Homo sapiens