Telomerase: Difference between revisions

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'''Overall Structure'''

Telomerase acts as both a monomer and dimer. The monomer refers to the overall protein and its catalytic subunit TERT, made up of an amino acid polymer. This protein binds with the RNA template, <scene name='60/602706/Ter/1'>TER</scene>, that TERT uses to add DNA to form a dimer-like structure. Both the protein and RNA components are highly conserved structures among phylogenetic groups. <scene name='60/602706/Tert/2'>TERT</scene> is organized into a ring-like structure that shares common features with other reverse transcriptases (in viruses for example) and DNA polymerases. The RNA-DNA heteroduplex lies in the interior of the ring and positions the 3' end of the DNA primer at the active site to the telomerse can be enlongated. The substrate binding within the ring can accomodate 7 to 8 bases of double-stranded nucleic acid.

<scene name='60/602706/Telomerase/1'>Telomerase</scene> (protein in blue; RNA in green; DNA in red) acts as both a monomer and dimer. The monomer refers to the overall protein and its catalytic subunit TERT, made up of an amino acid polymer. This protein binds with the RNA template, <scene name='60/602706/Ter/1'>TER</scene>, that TERT uses to add DNA to form a dimer-like structure. Both the protein and RNA components are highly conserved structures among phylogenetic groups. <scene name='60/602706/Tert/2'>TERT</scene> is organized into a ring-like structure that shares common features with other reverse transcriptases (in viruses for example) and DNA polymerases. The RNA-DNA heteroduplex lies in the interior of the ring and positions the 3' end of the DNA primer at the active site to the telomerse can be enlongated. The substrate binding within the ring can accomodate 7 to 8 bases of double-stranded nucleic acid.

== Active Site Chemistry ==

Telomerase: Difference between revisions

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@@ Line 14: / Line 14: @@
 '''Overall Structure'''
-Telomerase acts as both a monomer and dimer. The monomer refers to the overall protein and its catalytic subunit TERT, made up of an amino acid polymer. This protein binds with the RNA template, <scene name='60/602706/Ter/1'>TER</scene>, that TERT uses to add DNA to form a dimer-like structure. Both the protein and RNA components are highly conserved structures among phylogenetic groups. <scene name='60/602706/Tert/2'>TERT</scene> is organized into a ring-like structure that shares common features with other reverse transcriptases (in viruses for example) and DNA polymerases. The RNA-DNA heteroduplex lies in the interior of the ring and positions the 3' end of the DNA primer at the active site to the telomerse can be enlongated. The substrate binding within the ring can accomodate 7 to 8 bases of double-stranded nucleic acid.
+<scene name='60/602706/Telomerase/1'>Telomerase</scene> (protein in blue; RNA in green; DNA in red) acts as both a monomer and dimer. The monomer refers to the overall protein and its catalytic subunit TERT, made up of an amino acid polymer. This protein binds with the RNA template, <scene name='60/602706/Ter/1'>TER</scene>, that TERT uses to add DNA to form a dimer-like structure. Both the protein and RNA components are highly conserved structures among phylogenetic groups. <scene name='60/602706/Tert/2'>TERT</scene> is organized into a ring-like structure that shares common features with other reverse transcriptases (in viruses for example) and DNA polymerases. The RNA-DNA heteroduplex lies in the interior of the ring and positions the 3' end of the DNA primer at the active site to the telomerse can be enlongated. The substrate binding within the ring can accomodate 7 to 8 bases of double-stranded nucleic acid.
 == Active Site Chemistry ==