Abstract:
:The voltage-gated sodium channel (VGSC) is a complex, which is composed of one pore-forming α subunit and at least one β subunit. Up to now, five β subunits are known: β1/β1A, β1B, β2, β3, and β4, encoded by four genes (SCN1B∼SCN4B). It is critical to have a deep understanding of the interaction between β1 and β3 subunits, two subunits which frequently appear in many diseases concurrently. In this study, we had screened out the new template of β1 subunit for homology modelling, which shares higher similarity to β3. Docking studies of the β1 and β3 homology model were conducted, and likely β1 and β3 binding loci were investigated. The results revealed that β1-β3 is more likely to form a di-polymer than β1-β1 based on molecular interaction analysis, including potential energy analysis, Van der Waals (VDW) energy analysis and electrostatic energy analysis, and in addition, consideration of the hydrogen bonds and hydrophobic contacts that are involved. Based on these analyses, the residues His122 and Lys140 of β1 and Glu 66, Asn 131, Asp 118, Glu 120, Glu133, Asn135, Ser 137 of β3 were predicted to play a functional role.
journal_name
C R Bioljournal_title
Comptes rendus biologiesauthors
Liu Q,Jin Y,Wang K,Meng XX,Yang Y,Yang Z,Zhao YS,Zhao MY,Zhang JHdoi
10.1016/j.crvi.2013.11.009subject
Has Abstractpub_date
2014-02-01 00:00:00pages
73-7issue
2eissn
1631-0691issn
1768-3238pii
S1631-0691(13)00277-1journal_volume
337pub_type
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journal_title:Comptes rendus biologies
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journal_title:Comptes rendus biologies
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