C1orf41 Abstract: Difference between revisions
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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. | 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. | 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. | 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. | ||
Revision as of 21:55, 15 June 2009
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.
