Titin Structure & Function

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

Current revision

Rabbit titin molecule I65-I70 3b43

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3D structures of titin

Titin


References

  1. 1.0 1.1 1.2 1.3 1.4 Trinick J, Tskhovrebova L. Titin: a molecular control freak. Trends Cell Biol. 1999 Oct;9(10):377-80. PMID:10481174
  2. 2.00 2.01 2.02 2.03 2.04 2.05 2.06 2.07 2.08 2.09 2.10 2.11 2.12 2.13 2.14 2.15 2.16 2.17 2.18 2.19 2.20 Tskhovrebova L, Trinick J. Titin: properties and family relationships. Nat Rev Mol Cell Biol. 2003 Sep;4(9):679-89. PMID:14506471 doi:10.1038/nrm1198
  3. 3.0 3.1 Tskhovrebova L, Trinick J, Sleep JA, Simmons RM. Elasticity and unfolding of single molecules of the giant muscle protein titin. Nature. 1997 May 15;387(6630):308-12. PMID:9153398 doi:10.1038/387308a0
  4. von Castelmur E, Marino M, Svergun DI, Kreplak L, Ucurum-Fotiadis Z, Konarev PV, Urzhumtsev A, Labeit D, Labeit S, Mayans O. A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain. Proc Natl Acad Sci U S A. 2008 Jan 29;105(4):1186-91. Epub 2008 Jan 22. PMID:18212128
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