Biol. Bull.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF) Free
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schetz, J. A.
Right arrow Articles by Anderson, PAV.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Schetz, J. A.
Right arrow Articles by Anderson, PAV.

The Biological Bulletin, Vol 185, Issue 3 462-466, Copyright © 1993 by Marine Biological Laboratory


RESEARCH NOTE

A Reevaluation of the Structure in the Pore Region of Voltage-Activated Cation Channels

J. A. Schetz and PAV. Anderson
The Whitney Laboratory University of Florida, St. Augustine, Florida 32086

Members of the Voltage-Sensitive Cation Channel (VSCC) superfamily from highly selective voltage-gated pores in excitable membranes. These pores are thought to be formed from the extrucellulur loops thut interconnect transmembrane segments 5 und 6 in each of the four domains that constitute the channel. Each of these loops is currently modeled as consisting of two short segments, SS1 and SS2, that are linked by a hairpin turn to form an antiparallel structure. In this study, the hypothesized {beta}-turn in the S5-S6 loop of each of 80 domains from the VSCC superfumily (26 different channel isoforms) were identified and located on the basis of their significant local maxima for {beta}-turn propensity (Pbend). Significant {beta}-turns were identified in all 80 sequences, but they are shtifted, and lie in the region currently defined as the SS2 {beta}-strand. This location of the {beta}-turn is incompatible with an antiparallel {beta}-sheet structure of the pore. The region identified here as,forming the turn corresponds to the ion selective determinants in the pore, implying that the turn imparts some of the ionic selectivity of each channel.


This article has been cited by other articles:


Home page
Protein Eng Des SelHome page
G. Barreiro, C. R. W. Guimaraes, and R. B. de Alencastro
Potential of mean force calculations on an L-type calcium channel model
Protein Eng. Des. Sel., March 1, 2003; 16(3): 209 - 215.
[Abstract] [Full Text] [PDF]


Home page
Protein Eng Des SelHome page
G. Barreiro, C. R. W. Guimaraes, and R. B. de Alencastro
A molecular dynamics study of an L-type calcium channel model
Protein Eng. Des. Sel., February 1, 2002; 15(2): 109 - 122.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. E. Koch, I. Bodi, A. Schwartz, and G. Varadi
Architecture of Ca2+ Channel Pore-lining Segments Revealed by Covalent Modification of Substituted Cysteines
J. Biol. Chem., October 27, 2000; 275(44): 34493 - 34500.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by the Marine Biological Laboratory.