Difference between revisions of "PAS domain"
(→B. subtilis proteins containing a PAS domain) |
(→Important reviews) |
||
| Line 27: | Line 27: | ||
==Important reviews== | ==Important reviews== | ||
| − | <pubmed> 10357859 17824925 14668441 </pubmed> | + | <pubmed> 10357859 17824925 14668441 21663441</pubmed> |
= Back to [[Domains]] = | = Back to [[Domains]] = | ||
Revision as of 09:29, 22 September 2015
Contents
Introduction
The PAS domain is a protein domain contained in many signaling proteins where it functions as a signal sensor. PAS domains are found in a large number of organisms from bacteria to humans. The PAS domain was named after the three proteins in which it was first discovered:
- Per – period circadian protein
- Arnt – aryl hydrocarbon receptor nuclear translocator protein
- Sim – single-minded protein
B. subtilis proteins containing a PAS domain
Related SubtiWiki pages
Important reviews
Jonathan T Henry, Sean Crosson
Ligand-binding PAS domains in a genomic, cellular, and structural context.
Annu Rev Microbiol: 2011, 65;261-86
[PubMed:21663441]
[WorldCat.org]
[DOI]
(I p)
Barry L Taylor
Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy.
Mol Microbiol: 2007, 65(6);1415-24
[PubMed:17824925]
[WorldCat.org]
[DOI]
(P p)
Paul J A Erbel, Paul B Card, Ozgur Karakuzu, Richard K Bruick, Kevin H Gardner
Structural basis for PAS domain heterodimerization in the basic helix--loop--helix-PAS transcription factor hypoxia-inducible factor.
Proc Natl Acad Sci U S A: 2003, 100(26);15504-9
[PubMed:14668441]
[WorldCat.org]
[DOI]
(P p)
B L Taylor, I B Zhulin
PAS domains: internal sensors of oxygen, redox potential, and light.
Microbiol Mol Biol Rev: 1999, 63(2);479-506
[PubMed:10357859]
[WorldCat.org]
[DOI]
(P p)
