Titin Structure & Function - Revision history

Alexander Berchansky at 10:30, 11 July 2012

2012-07-11T10:30:04Z

← Older revision		Revision as of 10:30, 11 July 2012
Line 8:		Line 8:
	Titin, a polypeptide chain protein that is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multi-domain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately 300 Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. Titin being amulti-domain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>		Titin, a polypeptide chain protein that is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multi-domain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately 300 Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. Titin being amulti-domain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>

	~~<applet load='3b43' size='400' frame='true' align='right' caption='Rabbit titin molecule I65-I70 [[3b43]]' />~~

	== Function ==		== Function ==

Alexander Berchansky at 10:29, 11 July 2012

2012-07-11T10:29:51Z

← Older revision		Revision as of 10:29, 11 July 2012
Line 1:		Line 1:
			<StructureSection load='3b43' size='400' side='right' scene= caption='Rabbit titin molecule I65-I70 [[3b43]]' >


	Titin,also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today.<ref name=journal4/> Titins are a family of large proteins that which can be broken down into two subclasses of striated and non-muscle cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.		Titin,also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today.<ref name=journal4/> Titins are a family of large proteins that which can be broken down into two subclasses of striated and non-muscle cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.

Line 19:		Line 22:
	Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.		Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.

			</StructureSection>
	==3D structures of titin==		==3D structures of titin==

	[[Titin]]		[[Titin]]

	~~==Additional Resources==~~
	~~See: [[Titin]] for additional information <br />~~


	= References =		= References =
	<references/>		<references/>

Michal Harel at 07:59, 19 September 2011

2011-09-19T07:59:52Z

← Older revision		Revision as of 07:59, 19 September 2011
Line 5:		Line 5:
	Titin, a polypeptide chain protein that is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multi-domain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately 300 Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. Titin being amulti-domain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>		Titin, a polypeptide chain protein that is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multi-domain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately 300 Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. Titin being amulti-domain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>

	<applet load='3b43' size='400' frame='true' align='right' caption='~~Titin Molecule~~' />		<applet load='3b43' size='400' frame='true' align='right' caption='Rabbit titin molecule I65-I70 [[3b43]]' />

	== Function ==		== Function ==
Line 18:		Line 18:

	Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.		Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.

			==3D structures of titin==

			[[Titin]]

	==Additional Resources==		==Additional Resources==

Alexander Berchansky at 13:06, 30 December 2010

2010-12-30T13:06:02Z

← Older revision		Revision as of 13:06, 30 December 2010
Line 18:		Line 18:

	Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.		Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.

			==Additional Resources==
			See: [[Titin]] for additional information <br />


	= References =		= References =
	<references/>		<references/>

David Canner: Sandbox 183 moved to Titin Structure & Function

2010-10-18T06:48:46Z

Sandbox 183 moved to Titin Structure & Function

← Older revision	Revision as of 06:48, 18 October 2010
(No difference)

Merrick Sandhu at 06:02, 1 April 2010

2010-04-01T06:02:09Z

← Older revision		Revision as of 06:02, 1 April 2010
Line 1:		Line 1:
	Titin, also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today.<ref name=journal4/> Titins are a family of large proteins that which can be broken down into two subclasses of striated and ~~nonmuscle~~ cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.		Titin,also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today.<ref name=journal4/> Titins are a family of large proteins that which can be broken down into two subclasses of striated and non-muscle cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.

	== Overall Structure ==		== Overall Structure ==

	Titin is a polypeptide chain protein ~~which~~ is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a ~~multidomain~~ structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. ~~The multidomain~~ structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>		Titin, a polypeptide chain protein that is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multi-domain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately 300 Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. Titin being amulti-domain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>

	<applet load='3b43' size='400' frame='true' align='right' caption='Titin Molecule' />		<applet load='3b43' size='400' frame='true' align='right' caption='Titin Molecule' />
Line 9:		Line 9:
	== Function ==		== Function ==

	Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> The protein molecules plays a role in thick-filament and sacromere assembly.<ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends.<ref name=journal1/> It is known that both the Z-line and M-line ends of the titin molecules are parts of the signalling pathway that control tension and protein-turnover-related mechanisms.<ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation. It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules ~~have a~~ part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/>		Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> The protein molecules plays a role in thick-filament and sacromere assembly.<ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends.<ref name=journal1/> It is known that both the Z-line and M-line ends of the titin molecules are parts of the signalling pathway that control tension and protein-turnover-related mechanisms.<ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation.<ref name=journal1/> It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules is to take part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/>

	Titin that is intact has been found to be important for normal muscle structure and function.<ref name=journal1/> This was observed when titin mutation disrupted the sacromere assembly and function, an example would be mutations that affect the I-band portion of titin would change the elasticity of muscle.<ref name=journal1/>		Titin that is intact has been found to be important for normal muscle structure and function.<ref name=journal1/> This was observed when titin mutation disrupted the sacromere assembly and function, an example would be mutations that affect the I-band portion of titin would change the elasticity of muscle.<ref name=journal1/>

	Titin ~~has also been found to be~~ linked with chromosomes, having a key role in mitosis.<ref name=journal4/> During mitosis, titin control the axial diameter of mitotic chromosomes.<ref name=journal4/>		Titin linked with chromosomes, having a key role in mitosis.<ref name=journal4/> During mitosis, titin control the axial diameter of mitotic chromosomes.<ref name=journal4/>

	==Structure Related to Function==		==Structure Related to Function==

	Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The ~~way the~~ structure is the ~~only reason why it can work~~ as an elastic ~~for~~ muscles ~~for when they contract and release~~.		Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The structure is able to give an idea on how it relates to the function and how titin works as an elastic in muscles.

	= References =		= References =
	<references/>		<references/>

Merrick Sandhu at 22:12, 31 March 2010

2010-03-31T22:12:10Z

← Older revision		Revision as of 22:12, 31 March 2010
Line 1:		Line 1:
	Titin, also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today. Titins are a family of large proteins that which can be broken down into two subclasses of striated and nonmuscle cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.		Titin, also known as connectin, is a flexible intrasarcomeric filamentous protein, which is largest proteins known today.<ref name=journal4/> Titins are a family of large proteins that which can be broken down into two subclasses of striated and nonmuscle cells of vertebrates <ref name=journal4>PMID:10481174 </ref>.

	== Overall Structure ==		== Overall Structure ==

Merrick Sandhu at 21:06, 31 March 2010

2010-03-31T21:06:13Z

← Older revision		Revision as of 21:06, 31 March 2010
Line 13:		Line 13:
	Titin that is intact has been found to be important for normal muscle structure and function.<ref name=journal1/> This was observed when titin mutation disrupted the sacromere assembly and function, an example would be mutations that affect the I-band portion of titin would change the elasticity of muscle.<ref name=journal1/>		Titin that is intact has been found to be important for normal muscle structure and function.<ref name=journal1/> This was observed when titin mutation disrupted the sacromere assembly and function, an example would be mutations that affect the I-band portion of titin would change the elasticity of muscle.<ref name=journal1/>

	Titin has also been found to be linked with chromosomes, having a key role in mitosis.<ref name=journal4/> During mitosis, titin control the axial diameter of mitotic chromosomes.<ref name=journal4/>		Titin has also been found to be linked with chromosomes, having a key role in mitosis.<ref name=journal4/> During mitosis, titin control the axial diameter of mitotic chromosomes.<ref name=journal4/>

			==Structure Related to Function==

			Titin is a fairly linear protein with a reasoning to why the structure is that way. Titin being a filamentous shaped protein is able to its job in striated muscles.<ref name=journal4/> The molecules are formed with bands themselves and when they form sacromeres they line up next to one another in a linear fashion. The way the structure is the only reason why it can work as an elastic for muscles for when they contract and release.

	= References =		= References =
	<references/>		<references/>

Merrick Sandhu at 20:54, 31 March 2010

2010-03-31T20:54:22Z

← Older revision		Revision as of 20:54, 31 March 2010
Line 9:		Line 9:
	== Function ==		== Function ==

	Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends.<ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation. It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules have a part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/>		Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> The protein molecules plays a role in thick-filament and sacromere assembly.<ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends.<ref name=journal1/> It is known that both the Z-line and M-line ends of the titin molecules are parts of the signalling pathway that control tension and protein-turnover-related mechanisms.<ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation. It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules have a part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/>

			Titin that is intact has been found to be important for normal muscle structure and function.<ref name=journal1/> This was observed when titin mutation disrupted the sacromere assembly and function, an example would be mutations that affect the I-band portion of titin would change the elasticity of muscle.<ref name=journal1/>

			Titin has also been found to be linked with chromosomes, having a key role in mitosis.<ref name=journal4/> During mitosis, titin control the axial diameter of mitotic chromosomes.<ref name=journal4/>

	= References =		= References =
	<references/>		<references/>

Merrick Sandhu at 20:03, 31 March 2010

2010-03-31T20:03:29Z

← Older revision		Revision as of 20:03, 31 March 2010
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	== Overall Structure ==		== Overall Structure ==


	Titin is a polypeptide chain protein which is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multidomain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. The multidomain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>		Titin is a polypeptide chain protein which is greater than 1µm in length and 3-4 nm in width <ref name=journal1>PMID:14506471</ref>. The protein molecule has a molecular weight of up to approximately 4 Mda. Titin is a multidomain structure that which is found to be composed of two types of domains similar to immunoglobulin (Ig) and fibronectin.<ref name=journal2/> There are approximately Ig and fibronectin domains present in titin, with also kinase domains close to the carboxyl terminus.<ref name=journal1/> These two types of domains are β-sandwiches of seven or eight strands that are made of about 100 residues.<ref name=journal1/> The carboxyl terminus is in the head region of a titin molecule, the <scene name='Sandbox_183/N_to_c_terminus/3'>carboxyl terminus </scene>is represented as the red part molecule image.<ref name=journal1/> The structure also contains specialized binding sites and a putative elastic region, the PEVK domain, and there is a unique sequence region part of a titin molecule <ref name=journal2>PMID:9153398</ref>. The multidomain structure is evident by the interdomain periodicity seen in the structure.<ref name=journal1/> A titin molecule is half a sacromeres size with the four regions of the I-band,the A-band, the M-line and the Z-line. <ref name=journal1/> The I-band section of the titin is made up of only Ig domains and unique sequences with the Ig domains arranged in tandem.<ref name=journal1/> The A-band section is the largest part of the protein molecule with a highly conserved sequence.<ref name=journal1/> In the A-band section the Ig and fibronectin domains are set up in a long range pattern and are called the super repeats. There are two types of the Ig and fibronectin sets that are arranged in long range patterns, made from either seven and eleven domains. Located near the end of the A-band there are six copies of small super repeats, that which are 25-30 nm long. <ref name=journal1/> The M-line contains the overlapped carboxyl terminus regions of the titin molecule. <ref name=journal1/> The Z-line region is on the opposite end which has the overlapped amino terminal regions of a molecule from the neighboring sacromere.<ref name=journal1/>
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	<applet load='3b43' size='400' frame='true' align='right' caption='Titin Molecule' />		<applet load='3b43' size='400' frame='true' align='right' caption='Titin Molecule' />

			== Function ==

	== ~~Function~~ ==		Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends.<ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation. It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules have a part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/>

	Titin seems to be a key component in the assembly and functioning of vertebrates straited muscles.<ref name=journal1/> It has regions that mirror the different parts of the sacromere, which have mechanical functions, catalytic functions and the ability to bind many other sacromere proteins. <ref name=journal1/> Titin has a role in muscle signalling mechanisms, this was discovered from the kinase domain toward the carboxy-terminal, M-line end, and potential phosphorylation sites near both ends. <ref name=journal1/> Titin is also responsible for the elasticity of relaxed striated muscles and acts as the molecular scaffold for thick filament formation. It generates most of the elastic response of a sacromere, which responds like a bidirectional spring which stretches and recoils during movement of muscles to cause the myofibril to go back to its resting state <ref name=journal3>PMID:18212128</ref>. In mature muscle, titin molecules have a part in the mechanisms that control elasticity and the operating range (the length range of sacromeres when they shorten and extend in muscle in vivo) of sacromere lengths and tension-related processes in the body. <ref name=journal1/> A primary function of titin is giving elastic stabilization of relative positions of myosin and actin filaments.<ref name=journal1/>
	= References =		= References =
	<references/>		<references/>