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Literature DB >> 1713679

A molecular blueprint for the pore-forming structure of voltage-gated calcium channels.

Abstract

A protein that imitates the sequence of a highly conserved segment predicted to line the pore of dihydropyridine-sensitive L-type calcium channels was designed and synthesized. Single-channel conductance properties were studied in planar lipid bilayers. The synthetic protein emulates the ionic conductance, ionic selectivity, and pharmacological properties of the authentic calcium channel, including the stereospecific action of agonist and antagonist enantiomers of the dihydropyridine BayK 8644. The identified sequence is identical in L-type calcium channels from skeletal muscle and isoforms of cardiac muscle, brain, and aorta. It is plausible that this structural motif represents the molecular blueprint for the pore-forming structure of voltage-gated calcium channels.

Entities: Chemical

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Year: 1991 PMID： 1713679 PMCID： PMC52096 DOI： 10.1073/pnas.88.15.6418

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

33 in total

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11 in total

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Journal: Protein Sci Date: 1992-12 Impact factor: 6.725

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Journal: Biophys J Date: 1998-01 Impact factor: 4.033

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7. Two-dimensional 1H NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution.

Authors: J Gesell; M Zasloff; S J Opella
Journal: J Biomol NMR Date: 1997-02 Impact factor: 2.835

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Authors: Carl R Yamnitz; George W Gokel
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Journal: Biochem J Date: 1994-12-15 Impact factor: 3.857