C1orf41 Abstract: Difference between revisions

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Chromosome 1 open reading frame 41 (c1orf41) which was isolated from human placenta is an intracellular monomeric protein with 153 amino acids. This protein was encoded by gene on chromosome 1 locus 1p32.1-p33. The aim of this project is to predict the function of c1orf41 based on its sequence and structure by utilizing the various bioinformatics tools available. Blast result indicated that c1orf41 have high sequence similarity with small heat shock protein (sHsp).The sequence of alpha-B-crystallin domain that is conserved in sHsp as well as the beta-pleated sheet of alpha-B-crystallin was also found in c1orf41. On the other hand, DALI and Pfam suggested that our protein belongs to a discoidin (F5/8 C type) domain which is a galactose binding-like domain hence there is a possibility that c1orf41 involves in galactose binding. Besides that, discoidin domain is also known to be involve in cell adhesion. However, since the residues and position of the galactose binding site and the cell adhesion motif are not present in the sequence, this eliminates the possibility that c1orf41 is involved in galactose binding and cell adhesion. sHsp is an intracellular protein that is known to have chaperone function to prevent protein aggregation induced by thermal and chemical stress.It was also reported that sHsp has an anti apoptotic function by interacting with several programmed cell death machinery within the mitochondria. sHsp prevents the release of pro apoptotic molecules such as cytochrome c and caspase and this links to its high expression in cancer cells. Therefore, c1orf41 is more likely to be a sHsp.
Our protein target, isolated from human placenta, is chromosome 1 open reading frame 41 (c1orf41) which is an intracellular monomeric protein with 153 amino acids. C1orf41 protein was encoded by gene on chromosome 1 locus 1p32.1-p33.
 
Blast result indicated that our protein,c1orf41,has high sequence similarity with small heat shock protein (sHsp).The sequence of alpha-B-crystalline domain that is conserved in sHsp was found in our protein. Moreover, the beta-pleated sheet of alpha-B-crystalline also revealed in c1orf41 structure. On the other hand, the DALI and Pfam suggested that our protein belongs to a discoidin (F5/8 C type) domain which has similar structure with galactose binding function. Discoidin domain is known to function in cell adhesion.However, c1orf41 structure does not have a galactose binding and cell adhesion motif. Therefore, based on that information, the c1orf41 is more likely a sHsp.
 
sHsp is an intracellular protein that known to have chaperone function to prevent protein aggregation induced by thermal and chemical stress.It was also reported that sHsp has anti apoptotic function. It will interact with several programmed cell death machinery within mitochondria.sHsp prevent the release of pro apoptotic molecules such as cytochrome c and caspase.Thus,sHsps are highly express in cancer.
 
 





Latest revision as of 01:44, 16 June 2009

Chromosome 1 open reading frame 41 (c1orf41) which was isolated from human placenta is an intracellular monomeric protein with 153 amino acids. This protein was encoded by gene on chromosome 1 locus 1p32.1-p33. The aim of this project is to predict the function of c1orf41 based on its sequence and structure by utilizing the various bioinformatics tools available. Blast result indicated that c1orf41 have high sequence similarity with small heat shock protein (sHsp).The sequence of alpha-B-crystallin domain that is conserved in sHsp as well as the beta-pleated sheet of alpha-B-crystallin was also found in c1orf41. On the other hand, DALI and Pfam suggested that our protein belongs to a discoidin (F5/8 C type) domain which is a galactose binding-like domain hence there is a possibility that c1orf41 involves in galactose binding. Besides that, discoidin domain is also known to be involve in cell adhesion. However, since the residues and position of the galactose binding site and the cell adhesion motif are not present in the sequence, this eliminates the possibility that c1orf41 is involved in galactose binding and cell adhesion. sHsp is an intracellular protein that is known to have chaperone function to prevent protein aggregation induced by thermal and chemical stress.It was also reported that sHsp has an anti apoptotic function by interacting with several programmed cell death machinery within the mitochondria. sHsp prevents the release of pro apoptotic molecules such as cytochrome c and caspase and this links to its high expression in cancer cells. Therefore, c1orf41 is more likely to be a sHsp.




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