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The word strabismus is new latin, the from greek strabismos condition of squinting.
Strabismus (stbm) or Van Gogh (Vang) is a four pass transmembrane protein.
Bastock et al. 2003: The localisation of Strabismus-EYFP over time. Note the asymmetry of Strabismus as the cells reorganise.
Strabismus encodes a novel protein with four hydrophobic that inserts it into the plasma membrane (Wolff and Rubin, 1998). At the N terminus of the protein there are three amino acids that match the consensus for a PDZ-binding domain (PBM), this suggests that Strabismus might interact with PDZ-domain proteins.
Homologues for Stabismus are found all through the animal kingdom, and include worms, fish, frogs, mice and humans (Darken et al., 2002; Goto and Keller, 2002; Kibar et al., 2001; Park and Moon, 2002; Wolff and Rubin, 1998).
The structure of Strabismus
The structure of Strabismus
The structure of Strabismus was reported in 1998 (Wolfe and Rubin 1998). It was described as being a protein that does not share homology with other known proteins.
Strabismus is also pretty sparse when it comes to looking for known protein domains and it only has a putative PDZ domain-binding motif at its C-terminus. This has made it tricky to understand what Strabismus actually does. However, there are homologs of Strabismus found in mammals and worms, which indicates the function of Strabismus is conserved.
Was a structure and function analysis done to determine which regions are functionally important?
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