C1orf41 Discussion: Difference between revisions
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Based on Blast, it was shown that this protein has high similarity sequence with small heat shock proteins (sHsp) from various eukaryotes. Our protein was a mutant of sHsp family B member 11 where aspartic acid at position 109 has been deleted. The first ten residues were believed not to be part of the protein but most likely an N-terminal histidine tag used during purification of the protein. This was proven by the multiple sequence alignment as these residues does not align with organisms. Therefore, we hypothesized that c1orf41 may be a sHsp. | |||
sHsp are molecular chaperones that can be found in various organisms, however they are poorly conserved. Studies have shown that the number gene encoding sHsp increase in higher eukaryote. This may due to the specific function and localization of sHsp (Haslbeck ''et al''., 2005). Since it was shown to be highly expressed in cancer cell, the function of this protein may be related to cancer. | |||
Even though the structure showed similarity with galactose binding domain, the binding site of galactose was not found in c1orf41. This indicates that this protein does not bind to galactose. | Even though the structure showed similarity with galactose binding domain, the binding site of galactose was not found in c1orf41. This indicates that this protein does not bind to galactose. | ||
Revision as of 11:39, 10 June 2009
Based on Blast, it was shown that this protein has high similarity sequence with small heat shock proteins (sHsp) from various eukaryotes. Our protein was a mutant of sHsp family B member 11 where aspartic acid at position 109 has been deleted. The first ten residues were believed not to be part of the protein but most likely an N-terminal histidine tag used during purification of the protein. This was proven by the multiple sequence alignment as these residues does not align with organisms. Therefore, we hypothesized that c1orf41 may be a sHsp.
sHsp are molecular chaperones that can be found in various organisms, however they are poorly conserved. Studies have shown that the number gene encoding sHsp increase in higher eukaryote. This may due to the specific function and localization of sHsp (Haslbeck et al., 2005). Since it was shown to be highly expressed in cancer cell, the function of this protein may be related to cancer.
Even though the structure showed similarity with galactose binding domain, the binding site of galactose was not found in c1orf41. This indicates that this protein does not bind to galactose.
This protein was also hypothesized to be involved in cell adhesion. However, due to the lack of the RGD motif that is present in cell adhesion proteins hence we can deduce that this protein does not involve in cell adhesion (Bianchet et al., 2002).
