2gyd
From Proteopedia
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Complex of equine apoferritin with the H-diaziflurane photolabeling reagent
Overview
The difficulty in obtaining binding target and site information for, low-affinity drugs, like the inhaled anesthetics, has limited, identification of their molecular effectors. Because such information can, be provided by photoactive analogues, we designed, synthesized, and, characterized a novel diazirnyl haloether that closely mimics isoflurane, the most widely used clinical general anesthetic. This compound, H-diaziflurane, is a nontoxic, potent anesthetic that potentiates, GABA-gated ion channels in primary cultures of hippocampal neurons., Calorimetric and structural characterizations show that H-diaziflurane, binds a model anesthetic host protein with similar energetics as, isoflurane and forms photoadducts with residues lining the isoflurane, binding site. H-diaziflurane will be immediately useful for identifying, targets and sites important for the molecular pharmacology of the inhaled, haloether anesthetics.
About this Structure
2GYD is a Single protein structure of sequence from Equus caballus with CD and DFE as ligands. Full crystallographic information is available from OCA.
Reference
Photoactive analogues of the haloether anesthetics provide high-resolution features from low-affinity interactions., Xi J, Liu R, Rossi MJ, Yang J, Loll PJ, Dailey WP, Eckenhoff RG, ACS Chem Biol. 2006 Jul 21;1(6):377-84. PMID:17163775
Page seeded by OCA on Wed Nov 21 11:27:36 2007
Categories: Equus caballus | Single protein | Eckenhoff, R. | Loll, P.J. | Rossi, M.J. | CD | DFE | Anesthetic | Helical bundles | Isoflurane
