Publication Date:
1999-02-19
Description:
Gap junction membrane channels mediate electrical and metabolic coupling between adjacent cells. The structure of a recombinant cardiac gap junction channel was determined by electron crystallography at resolutions of 7.5 angstroms in the membrane plane and 21 angstroms in the vertical direction. The dodecameric channel was formed by the end-to-end docking of two hexamers, each of which displayed 24 rods of density in the membrane interior, which is consistent with an alpha-helical conformation for the four transmembrane domains of each connexin subunit. The transmembrane alpha-helical rods contrasted with the double-layered appearance of the extracellular domains. Although not indicative for a particular type of secondary structure, the protein density that formed the extracellular vestibule provided a tight seal to exclude the exchange of substances with the extracellular milieu.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Unger, V M -- Kumar, N M -- Gilula, N B -- Yeager, M -- New York, N.Y. -- Science. 1999 Feb 19;283(5405):1176-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Scripps Research Institute, Department of Cell Biology, 10550 North Torrey Pines Road, Division of Cardiovascular Diseases, Scripps Clinic, 10666 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10024245" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Cell Line
;
Connexin 43/*chemistry
;
Cricetinae
;
Crystallography
;
Gap Junctions/*chemistry/ultrastructure
;
Lipid Bilayers/chemistry
;
Models, Molecular
;
Mutation
;
Myocardium/*chemistry/ultrastructure
;
Protein Conformation
;
*Protein Structure, Secondary
;
Recombinant Proteins/chemistry
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
