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Cell Commun Adhes. 2008 May;15(1):85-93. doi: 10.1080/15419060802013588.

Projection structure of a N-terminal deletion mutant of connexin 26 channel with decreased central pore density.

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1
Department of Biophysics, Faculty of Science, Kyoto University, Kyoto, Japan.

Abstract

Gated gap junction channels are important cellular conduits for establishing and maintaining intercellular communication. The three-dimensional structure of a mutant human connexin 26 (Cx26M34A) by electron cryocrystallography revealed a plug-like density in the channel pore suggesting that physical blockage of the pore may be one mechanism of closure (Oshima et al. 2007, Proc Natl Acad Sci USA 104: 10034-10039). However, it remains to be determined what part of the sequence contributes to the plug. Here, we present the projection structure of an N-terminus deletion of Cx26M34A missing amino acids 2 to 7 (Cx26M34Adel2-7) crystallized in the same two-dimensional crystal form. A 10 A resolution projection map of Cx26M34Adel2-7 revealed that the plug density was dramatically reduced in comparison with that found in full-length Cx26 channel. The difference map between the deletion and full-length Cx26M34A channels strongly suggests that the N-terminus of connexin contributes to the plug for the physical closure of gap junction channels.

PMID:
18649181
PMCID:
PMC2527467
DOI:
10.1080/15419060802013588
[Indexed for MEDLINE]
Free PMC Article
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