The scleraxis protein is a member of the basic-helix-loop-helix (bHLH) superfamily of transcription factors. Currently two genes (and respectively) have been identified to code for identical scleraxis proteins.
These helices have important functional properties, forming part of the DNA binding and transcription activating domains. With respect to scleraxis, the bHLH region spans amino acid residues 78 to 131. A proline rich region is also predicted to lie between residues 161-170. A stretch of basic residues, which aids in DNA binding, is found closer to the N terminal end of scleraxis.
HLH proteins that lack this basic domain have been shown to negatively regulate the activities of bHLH proteins and are called inhibitors of differentiation (Id). Basic HLH proteins function normally as dimers and bind to a specific hexanucleotide DNA sequence (CAANTG) known as an E-box thus switching on the expression of various genes involved in cellular development and survival.
WIPO ASSIGNS PATENT OF UNIVERSITY OF MANITOBA FOR "MODULATION OF SCLERAXIS USING A DOMINANT NEGATIVE SCLERAXIS MUTANT WITH A BASIC DNA-BINDING DOMAIN DELETION" (CANADIAN INVENTOR)
Nov 25, 2011; GENEVA, Nov. 23 -- Publication No. WO/2011/140639 was published on Nov. 17. Title of the invention: "MODULATION OF...