2gyd

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[[Image:2gyd.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_2gyd| PDB=2gyd | SCENE= }}
{{STRUCTURE_2gyd| PDB=2gyd | SCENE= }}
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'''Complex of equine apoferritin with the H-diaziflurane photolabeling reagent'''
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===Complex of equine apoferritin with the H-diaziflurane photolabeling reagent===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17163775 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17163775}}
==About this Structure==
==About this Structure==
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[[Category: Helical bundle]]
[[Category: Helical bundle]]
[[Category: Isoflurane]]
[[Category: Isoflurane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:39:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:53:15 2008''

Revision as of 14:53, 27 July 2008

Template:STRUCTURE 2gyd

Complex of equine apoferritin with the H-diaziflurane photolabeling reagent

Template:ABSTRACT PUBMED 17163775

About this Structure

2GYD is a Single protein structure of sequence from Equus caballus. 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

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