What are protein domains?
Protein domains are smaller, functional units of a gene that work together to create the overall function of the gene. Domains can also function on their own independently, are evolutionary conserved and can be categorized into Super families, families and subfamilies. Understanding how domains work separately can help us understand how the gene will function and interact in the body as a whole.
What protein domains are present in MSTN?
All techniques found that there were 2 domains within the MSTN gene: TGFb propeptide and TGFB. TGFB is a cytokine belonging to the the transforming growth factor super family and is responsible for the activation of other substrates and regulatory proteins. When TGFB is cleaved from the rest of the gene, TGFB works as a transcription factor that activates the synthesis of a protein called myostatin. Myostatin is a regulator of skeletal muscle maturation. TGFb propeptide is a latency peptide, associated with TGFB.
From the function of these domains we can infer that, when they are activated, are involved in the regulation of growth in a body system. Because it has been previously determined that a mutated or dysfunctional myostatin protein results in the overgrowth of skeletal muscle, we know that in this particular case, these domains are crucial for the regulation of skeletal muscle build up.
We can also see that the domains in other homologs such as mice, rat, frog and chimpanzee are highly conserved. Because of this high level of conservation, we can infer that these genes and their domains work in the body similarly to how they present in the human body.
Using InterPro and PFAM, we can see that these genes have the same domains with similar spacing as well as the same or close to the same amount of amino acids. Because of this, we can conclude that these homologs make the best candidates to use as model organisms when studying the MSTN gene.
References
[1] Massagué J (October 2012). "TGFβ signalling in context". Nature Reviews. Molecular Cell Biology. 13 (10): 616–30. doi:10.1038/nrm3434. PMC 4027049Freely accessible. PMID 22992590.
[2] Richardson J. S. (1981). "The anatomy and taxonomy of protein structure". Adv Protein Chem. 34: 167–339. doi:10.1016/S0065-3233(08)60520-3. PMID 7020376.
[2] Richardson J. S. (1981). "The anatomy and taxonomy of protein structure". Adv Protein Chem. 34: 167–339. doi:10.1016/S0065-3233(08)60520-3. PMID 7020376.
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