Top Module Empty

Bookmark Us




Print E-mail
PAS Domain
Structure:

No ImageThe PAS domains consists of a conserved α/β-fold with no obvious conservation in amino acid sequence. The common fold of PAS domains is characterized by several α-helices flanking a five-stranded anti-parallel β-sheet. There are a few conserved residues that form part of the hydrophobic core located around αA. The loops at the αA/αB segment is important for ligand binding.
Structure Reference:
Morais Cabral, J.H. et al. (1998) Cell 95(5), 649-655.
Erbel, PJ. et al. (2003) PNAS. 100(26): 15504-15509. PDB: 1P97.
Domain binding and function:
PAS (Per-ARNT-Sim) domains are modules found in all Kingdoms, first identified in the Drosophila protein PER and ARNT.  The PAS domains consists of a conserved α/β-fold with no obvious conservation in amino acid sequence.   PAS domains have important roles as sensory modules for oxygen tension, redox potential or light intensities.   The domain functions through protein-protein interactions or through binding cofactors within their hydrophobic cores to regulate protein-protein interactions in response to stimuli.   For HIFα, in response to hypoxic conditions, the PAS-B domain heterodimerizes with PAS-B of ARNT which is mediated by the basic helix-loop-helix leading to transcriptional activation.   The PAS domain for PASK, is a regulatory sensor that has a compound and ligand binding region that initiates a switch for regulating the kinase activity.
Examples of Proteins: 
PAS domain proteins
Binding partner
Consensus binding motif
HIFα

ARNT (HIFβ)

PASK

HERG

NCoA-1

STAT6
LXXLL

 
< Prev   Next >
© 2016 The Pawson Lab
Joomla! is Free Software released under the GNU/GPL License.