Titin: Difference between revisions

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As seen in the image (Z1Z2 / Telethonin complex), the major force enduring component of this complex is an elaborate intermolecular hydrogen bonding network formed across <scene name='2a38/Test/2'>β-strand</scene> among telethonin and Z1Z2 domains, and not intramolecularly among termini β-strands of individual Z1 or Z2 domains. This shift to a stronger force enduring interface reduces the possibility of unraveling the individual Ig-domains, thus stabilizing the complex. This demonstrates how <scene name='2a38/Test/2'>β-strand</scene> cross-linking via [http://en.wikipedia.org/wiki/Hydrogen_bonds hydrogen bonds] serves as an important mechanism. It functions as a molecular adhesive, increasing the ability of protein complexes to resist against mechanical stress.
As seen in the image (Z1Z2 / Telethonin complex), the major force enduring component of this complex is an elaborate intermolecular hydrogen bonding network formed across <scene name='2a38/Test/2'>β-strand</scene> among telethonin and Z1Z2 domains, and not intramolecularly among termini β-strands of individual Z1 or Z2 domains. This shift to a stronger force enduring interface reduces the possibility of unraveling the individual Ig-domains, thus stabilizing the complex. This demonstrates how <scene name='2a38/Test/2'>β-strand</scene> cross-linking via [http://en.wikipedia.org/wiki/Hydrogen_bonds hydrogen bonds] serves as an important mechanism. It functions as a molecular adhesive, increasing the ability of protein complexes to resist against mechanical stress.
==Disease==
See [[Titin related diseases]].


== 3D Structures of Titin ==
== 3D Structures of Titin ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
[[Titin 3D structures]]
 
[[2a38]], [[6fwx]], [[6sdb]] - hTTN residues 1-194 - human<br />
[[2f8v]], [[1ya5]] - hTTN residues 1-196+telethonin<br />
[[6dl4]] – hTTN residues 1821-1931 - NMR<br />
[[1g1c]] - hTTN residues 2027-2125<br />
[[5jdd]], [[5jde]] – hTTN  I9-I11 residues 2795-3053<br />
[[4qeg]], [[5jdj]] - hTTN I10 residues 2880-2967<br />
[[1tit]], [[1tiu]]- hTTN I27 residues 5253-5341 – NMR<br />
[[5joe]] - hTTN I81 residues 9582-9671<br />
[[2rq8]] – hTTN residues 12677-12765 (mutant) – NMR<br />
[[1waa]] - hTTN residues 12801-12889<br />
[[4o00]] - hTTN residues 14217-14319<br />
[[1bpv]] – hTTN A71 residues 14859-14961 – NMR<br />
[[3lpw]] – hTTN A77-A78 residues 22877-23070<br />
[[5bs0]] – hTTN  residues 24337-24345 + TCR<br />
[[2j8h]], [[2j8o]], [[2ill]] – hTTN  residues 24430-24623<br />
[[1tki]] – hTTN serine kinase fragment residues 24748-25068<br />
[[2bk8]] – hTTN residues 25073-25166<br />
[[1nct]], [[1ncu]] – hTTN M5 residues 26059-26155 – NMR<br />
[[1tnm]], [[1tnn]] – hTTN M5 residues 26059-26155<br />
[[3lcy]] – hTTN A164-A165 residues 31456-31649<br />
[[2nzi]] – hTTN residues 31854-32155<br />
[[4jnw]] - hTTN residues 32172-32492<br />
[[6hci]] - hTTN M3 residues 32712-32816<br />
[[3qp3]], [[6h4l]] – hTTN M4 residues 33294-33395<br />
[[3puc]] – hTTN M7 residues 33774-33871<br />
[[2y9r]], [[3q5o]] – hTTN M10 residues 34252-34350<br />
[[2wp3]], [[2wwm]], [[3knb]] – hTTN M10 residues 34252-34350 +obscurin-like protein 1 fragment <br />
[[2wwk]] - hTTN M10 residues 34252-34350 +obscurin-like protein 1 fragment (mutant) <br />
[[4c4k]], [[4uow]] - hTTN M10 residues 34252-34350 +obscurin IG domain<br />
[[2rik]] – rTTN I67-I69 – rabbit<br />
[[2rjm]] - rTTN I67-I69 (mutant)<br />
[[3b43]] - rTTN I65-I70<br />
[[1h8b]] – rTTN residues 648-698 + hα Actinin 2 EF hands 3&4<br />
[[6i0y]] – TTN I27 residues 14318-14406 in 50S ribosome – ''Escherichia coli'' – Cryo EM<br />
==Additional Resources==
==Additional Resources==
See: [[Titin Structure & Function]] for additional information <br />
See: [[Titin Structure & Function]] for additional information <br />

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, David Canner, Michal Harel, Jaime Prilusky