1exb: Difference between revisions

Revision as of 02:09, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1exb.png

Template:STRUCTURE 1exb

STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELSSTRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS

Template:ABSTRACT PUBMED 10884227

About this StructureAbout this Structure

1EXB is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels., Gulbis JM, Zhou M, Mann S, MacKinnon R, Science. 2000 Jul 7;289(5476):123-7. PMID:10884227

Page seeded by OCA on Tue Jul 1 02:09:48 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS'''
+===STRUCTURE OF THE CYTOPLASMIC BETA SUBUNIT-T1 ASSEMBLY OF VOLTAGE-DEPENDENT K CHANNELS===
-==Overview==
+<!--
-The structure of the cytoplasmic assembly of voltage-dependent K+ channels was solved by x-ray crystallography at 2.1 angstrom resolution. The assembly includes the cytoplasmic (T1) domain of the integral membrane alpha subunit together with the oxidoreductase beta subunit in a fourfold symmetric T1(4)beta4 complex. An electrophysiological assay showed that this complex is oriented with four T1 domains facing the transmembrane pore and four beta subunits facing the cytoplasm. The transmembrane pore communicates with the cytoplasm through lateral, negatively charged openings above the T1(4)beta4 complex. The inactivation peptides of voltage-dependent K(+) channels reach their site of action by entering these openings.
+The line below this paragraph, {{ABSTRACT_PUBMED_10884227}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10884227 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10884227}}
 ==About this Structure==
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 [[Category: Ion channel]]
 [[Category: Oxidoreductase]]
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