Telomerase Reverse Transcriptase - Revision history

Michal Harel at 21:22, 24 September 2018

2018-09-24T21:22:25Z

←Older revision		Revision as of 21:22, 24 September 2018
Line 69:		Line 69:
	==3D structures of telomerase reverse transcriptase==		==3D structures of telomerase reverse transcriptase==

-	See [[~~Reverse transcriptase~~]]	+	See [[Telomerase]]

	=='''Additional Resources'''==		=='''Additional Resources'''==

Michal Harel at 09:07, 24 September 2014

2014-09-24T09:07:20Z

←Older revision		Revision as of 09:07, 24 September 2014
Line 69:		Line 69:
	==3D structures of telomerase reverse transcriptase==		==3D structures of telomerase reverse transcriptase==

-	~~Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}~~	+	See [[Reverse transcriptase]]
-		+
-	[[~~2b2a~~]] ~~– TtTERT TEN domain – ''Tetrahymena thermophila''<br />~~	+
-	~~[[2r4g]] - TtTERT RNA-binding domain<br />~~	+
-	~~[[3du5]], [[3du6]] – TcTERT catalytic subunit – ''Tribolium castaneum''<br />~~	+
-	~~[[3kyl]] - TcTERT catalytic subunit + DNA + RNA<br />~~	+
-	~~[[4lmo]] – TERT RNA-binding domain – tiger puffer<br />~~	+
-	~~[[4o26]] – TERT RNA-binding domain + RNA – rice fish<br />~~	+

	=='''Additional Resources'''==		=='''Additional Resources'''==

Michal Harel at 07:26, 15 May 2014

2014-05-15T07:26:38Z

←Older revision		Revision as of 07:26, 15 May 2014
Line 68:		Line 68:

	==3D structures of telomerase reverse transcriptase==		==3D structures of telomerase reverse transcriptase==
		+
		+	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}

	[[2b2a]] – TtTERT TEN domain – ''Tetrahymena thermophila''<br />		[[2b2a]] – TtTERT TEN domain – ''Tetrahymena thermophila''<br />
	[[2r4g]] - TtTERT RNA-binding domain<br />		[[2r4g]] - TtTERT RNA-binding domain<br />
	[[3du5]], [[3du6]] – TcTERT catalytic subunit – ''Tribolium castaneum''<br />		[[3du5]], [[3du6]] – TcTERT catalytic subunit – ''Tribolium castaneum''<br />
-	[[3kyl]] - TcTERT catalytic subunit + DNA + RNA	+	[[3kyl]] - TcTERT catalytic subunit + DNA + RNA<br />
-		+	[[4lmo]] – TERT RNA-binding domain – tiger puffer<br />
		+	[[4o26]] – TERT RNA-binding domain + RNA – rice fish<br />

	=='''Additional Resources'''==		=='''Additional Resources'''==

Alexander Berchansky at 06:47, 22 September 2011

2011-09-22T06:47:53Z

←Older revision		Revision as of 06:47, 22 September 2011
Line 86:		Line 86:

	This page was created with content from a page authored by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].		This page was created with content from a page authored by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].
		+	[[Category:Topic Page]]

Michal Harel at 07:38, 19 September 2011

2011-09-19T07:38:17Z

←Older revision		Revision as of 07:38, 19 September 2011
Line 17:		Line 17:
	== '''Experimental fragment with TEN''' ==		== '''Experimental fragment with TEN''' ==

-	<applet load='2b2a' size='400' frame='true' align='right' caption='Tetrahymena thermophila telomerase reverse transcriptase TEN domain' scene='Sandbox/Presentation/3' />	+	<applet load='2b2a' size='400' frame='true' align='right' caption='Tetrahymena thermophila telomerase reverse transcriptase TEN domain [[2b2a]]' scene='Sandbox/Presentation/3' />
	A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.		A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.
	This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.		This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.
Line 66:		Line 66:
	Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.		Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.
	Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.		Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.
		+
		+	==3D structures of telomerase reverse transcriptase==
		+
		+	[[2b2a]] – TtTERT TEN domain – ''Tetrahymena thermophila''<br />
		+	[[2r4g]] - TtTERT RNA-binding domain<br />
		+	[[3du5]], [[3du6]] – TcTERT catalytic subunit – ''Tribolium castaneum''<br />
		+	[[3kyl]] - TcTERT catalytic subunit + DNA + RNA
		+

	=='''Additional Resources'''==		=='''Additional Resources'''==

Michal Harel at 07:35, 19 September 2011

2011-09-19T07:35:11Z

←Older revision		Revision as of 07:35, 19 September 2011
Line 17:		Line 17:
	== '''Experimental fragment with TEN''' ==		== '''Experimental fragment with TEN''' ==

-	<applet load='2b2a' size='400' frame='true' align='right' caption='''Tetrahymena thermophila'' telomerase reverse transcriptase TEN domain' scene='Sandbox/Presentation/3' />	+	<applet load='2b2a' size='400' frame='true' align='right' caption='Tetrahymena thermophila telomerase reverse transcriptase TEN domain' scene='Sandbox/Presentation/3' />
	A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.		A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.
	This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.		This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.

Michal Harel at 07:34, 19 September 2011

2011-09-19T07:34:42Z

←Older revision		Revision as of 07:34, 19 September 2011
Line 17:		Line 17:
	== '''Experimental fragment with TEN''' ==		== '''Experimental fragment with TEN''' ==

-	<applet load='2b2a' size='400' frame='true' align='right' caption='~~Insert caption here~~' scene='Sandbox/Presentation/3' />	+	<applet load='2b2a' size='400' frame='true' align='right' caption='''Tetrahymena thermophila'' telomerase reverse transcriptase TEN domain' scene='Sandbox/Presentation/3' />
	A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.		A Tetrahymena Thermophila TERT fragment consisting of residues 2-191 with an N-terminal His6 tag was cristallized in space group P3 with <scene name='Sandbox/Three/1'>three</scene> TERT molecules present in the crystallographic asymmetric unit.
	This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.		This 23.5-kDa fragment contains only one methionine residue, making phasing by substitution with selenomethionine (SeMet) difficult.

David Canner at 07:03, 3 October 2010

2010-10-03T07:03:38Z

←Older revision		Revision as of 07:03, 3 October 2010
Line 67:		Line 67:
	Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.		Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.

-	==Additional Resources==	+	=='''Additional Resources'''==
	For additional information, See: [[Cancer]]		For additional information, See: [[Cancer]]
	<br />		<br />

David Canner at 07:03, 3 October 2010

2010-10-03T07:03:17Z

←Older revision		Revision as of 07:03, 3 October 2010
Line 66:		Line 66:
	Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.		Development of cancer chemotherapeutics directed against the reverse-transcriptase domain of telomerase has been challenging, perhaps because the enzyme needs only low activity to maintain telomeres.
	Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.		Because the TEN domain is essential for telomerase activity and its structure seems to be conserved trough evolution, this portion of TERT is a potential new target for antitelomerase compounds.
		+
		+	==Additional Resources==
		+	For additional information, See: [[Cancer]]
		+	<br />

	== '''References''' ==		== '''References''' ==

Eran Hodis: /* User contributions */

2010-02-04T12:32:41Z

User contributions

←Older revision		Revision as of 12:32, 4 February 2010
Line 73:		Line 73:
	==User contributions==		==User contributions==

-	This page was created with content ~~taken~~ from a page by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].	+	This page was created with content from a page authored by [[User:Tanja Emmerich]] and [[User:Vinzenz Alejandro Bayro Kaiser]].