Chromosome 1 open reading frame 41 Function: Difference between revisions

From MDWiki
Jump to navigationJump to search
No edit summary
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''C1orf41'''
'''C1orf41'''


Based on Blast result, our protein has high similarity with sHsp, specifically with sHsp 16.2. Thus, they may have similar function.
*Based on Blast result, our protein has high similarity with sHsp, specifically with sHsp 16.2.
*Based on Pfam result, our protein target is a member of F5/8 type C (discoidin)domain.  


[[Image:GO.png|centre|framed|]]




'''sHsp function:'''
'''sHsp function:'''
1. Molecular chaperone function
1. Molecular chaperone function
Under cellular stress (heat or chemical stress), sHsp will prevent protein aggregation and precipitation by interact with & stabilize the targeted protein.  
Under cellular stress (heat or chemical stress), sHsp will prevent protein aggregation and precipitation by interact with & stabilize the targeted protein.  


Line 12: Line 17:


2. Cytoprotective Function
2. Cytoprotective Function
sHsp inhibit cell deaths by:
* Stabilizing the mitochondria system
sHsp interact with various component of programmed cell death machinery. It prevent the release of proapoptotic protein (caspase-3 and cytochrome c)within the mitochondria.
* Increasing the Akt phosphorylation.
Akt is a cytoprotective protein kinase which inactivates the tumor suppressor through phosphorylation-dependent process.
Based on the structure analysis, C1orf41 has a loop which binds to Ca2+.
The presence of Ca2+ presumably related to Akt phosphorylation (support the phosphorylation).




Based on experimental evidence, there was an interaction between c1orf41 and RAYL (Ras-like-GTPase superfamily member).
[[Image:string-evidence view.png|centre|framed|]]




Some articles about HSPB11 suggest that small heat shock protein play a role in development of cancer. Small hsp has anti apoptotic activity which if oer expressed lead to tumor growth and resistance to chemo or radiotheraphy (Bellyei ''et al'', 2006; Pozsgai'' et al'', 2007). The anti apoptotic effect of hsp is mediated by the activation of Hsp90 (which Hsp 16.2 binds with) and by the activation of PI-3 kinase-Akt pathway. Pozsgai ''et al'' (2007) research data suggest that there is correlation between the progressive cytolasmic of small hsp and brain tumor malignancy.
* Overexpression of Ras GTPase activating protein will enhance the phosphorylation & activity of Akt.  


'''sHsp play as antiapoptotic protein. Thus, it is highly express in cancer'''


The result of Blast search vs UniProt showed that 1tvg has the highest percentage identity (99 %)to chromosome 1 open reading frame 41, isoform CRA_b of ''Homo sapiens''.


[[Image:blast search vs uniprot.jpg]]
-----






'''Discoidin'''


STRING result: Predicted protein-protein interaction
"Proteins from discoidin domain commonly function as cellsurface-attached carbohydrate residues, proteins and lipids' (Hidai ''et al'', 2007).


[[Image:string result.jpg]]
*Discoidin first described as lectins with high affinity for galactose


New member:
*Discoidin factor V and VIII, functions as coagulation factor
*F5/8 type C domain, function as cell-cell interaction and recognition


'''However, discoidin is an extracellular protein, while c1orf41 is intracellular. Thus, c1orf41 is more likely a sHsp.'''




[[Image:interpro result.jpg]]


Based on Pfam result, the domain of our protein target (1tvg) is F5/8 (discoidin). Discoidin is blood coagulation factor V and VIII which contain in C terminal.


[[Image:Pfam result.jpg]]


[[Chromosome 1 open reading frame 41|Back to main page]]
[[Chromosome 1 open reading frame 41|Back to main page]]

Latest revision as of 05:09, 16 June 2009

C1orf41

  • Based on Blast result, our protein has high similarity with sHsp, specifically with sHsp 16.2.
  • Based on Pfam result, our protein target is a member of F5/8 type C (discoidin)domain.


GO.png


sHsp function:

1. Molecular chaperone function

Under cellular stress (heat or chemical stress), sHsp will prevent protein aggregation and precipitation by interact with & stabilize the targeted protein.

Bellyei et al(2007) tested the chaperoning function of sHsp 16.2. They determined the thermal resistance of E. coli over-expressing sHsp 16.2 or aHsp27. The result showed that the sHsp 16.2 over expressing E. coli were resistant against heat stress (increase number of surviving colonies) compared to E. coli not expressing sHsp.

2. Cytoprotective Function

sHsp inhibit cell deaths by:

  • Stabilizing the mitochondria system

sHsp interact with various component of programmed cell death machinery. It prevent the release of proapoptotic protein (caspase-3 and cytochrome c)within the mitochondria.

  • Increasing the Akt phosphorylation.

Akt is a cytoprotective protein kinase which inactivates the tumor suppressor through phosphorylation-dependent process.

Based on the structure analysis, C1orf41 has a loop which binds to Ca2+. The presence of Ca2+ presumably related to Akt phosphorylation (support the phosphorylation).


Based on experimental evidence, there was an interaction between c1orf41 and RAYL (Ras-like-GTPase superfamily member).

String-evidence view.png


  • Overexpression of Ras GTPase activating protein will enhance the phosphorylation & activity of Akt.

sHsp play as antiapoptotic protein. Thus, it is highly express in cancer




Discoidin

"Proteins from discoidin domain commonly function as cellsurface-attached carbohydrate residues, proteins and lipids' (Hidai et al, 2007).

  • Discoidin first described as lectins with high affinity for galactose

New member:

  • Discoidin factor V and VIII, functions as coagulation factor
  • F5/8 type C domain, function as cell-cell interaction and recognition

However, discoidin is an extracellular protein, while c1orf41 is intracellular. Thus, c1orf41 is more likely a sHsp.



Back to main page