3lut: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:3lut.png|left|200px]] | [[Image:3lut.png|left|200px]] | ||
Line 20: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
[[3lut]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LUT OCA]. | |||
==Reference== | ==Reference== | ||
Line 48: | Line 47: | ||
[[Category: Voltage gating]] | [[Category: Voltage gating]] | ||
[[Category: Voltage-gated channel]] | [[Category: Voltage-gated channel]] | ||
Revision as of 23:13, 14 March 2011
A Structural Model for the Full-length Shaker Potassium Channel Kv1.2A Structural Model for the Full-length Shaker Potassium Channel Kv1.2
Template:ABSTRACT PUBMED 20534430
About this StructureAbout this Structure
3lut is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Chen X, Wang Q, Ni F, Ma J. Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc Natl Acad Sci U S A. 2010 Jun 3. PMID:20534430
- ↑ Long SB, Campbell EB, Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science. 2005 Aug 5;309(5736):897-903. Epub 2005 Jul 7. PMID:16002581
- ↑ Long SB, Tao X, Campbell EB, MacKinnon R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature. 2007 Nov 15;450(7168):376-82. PMID:18004376 doi:http://dx.doi.org/10.1038/nature06265
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Pages with broken file links
- Rattus norvegicus
- Chen, X.
- Ma, J.
- Ni, F.
- Wang, Q.
- Gating charge
- Glycoprotein
- Ion transport
- Ionic channel
- Kv1 2
- Lipoprotein
- Membrane
- Membrane protein
- Nadp
- Normal-mode analysis
- Palmitate
- Phosphoprotein
- Potassium
- Potassium channel
- Potassium transport
- Transmembrane
- Transport
- Voltage gating
- Voltage-gated channel