1la0

<StructureSection load='1la0' size='340' side='right'caption='[[1la0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1la0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LA0 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mxl|1mxl]], [[1fi5|1fi5]]</div></td></tr>

[[https://www.uniprot.org/uniprot/TNNC1_CHICK TNNC1_CHICK]] Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments.

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== Publication Abstract from PubMed ==

Cardiac troponin C (TnC) is composed of two globular domains connected by a flexible linker. In solution, linker flexibility results in an ill defined orientation of the two globular domains relative to one another. We have previously shown a decrease in linker flexibility in response to cardiac troponin I (cTnI) binding. To investigate the relative orientation of calcium-saturated TnC domains when bound to cTnI, (1)H-(15)N residual dipolar couplings were measured in two different alignment media. Similarity in alignment tensor orientation for the two TnC domains supports restriction of domain motion in the presence of cTnI. The relative spatial orientation of TnC domains bound to TnI was calculated from measured residual dipolar couplings and long-range distance restraints utilizing a rigid body molecular dynamics protocol. The relative domain orientation is such that hydrophobic pockets face each other, forming a latch to constrain separate helical segments of TnI. We have utilized this structure to successfully explain the observed functional consequences of linker region deletion mutants. Together, these studies suggest that, although linker plasticity is important, the ability of TnC to function in muscle contraction can be correlated with a preferred domain orientation and interdomain distance.

Solution structure of calcium-saturated cardiac troponin C bound to cardiac troponin I.,Dvoretsky A, Abusamhadneh EM, Howarth JW, Rosevear PR J Biol Chem. 2002 Oct 11;277(41):38565-70. Epub 2002 Jul 29. PMID:12147696<ref>PMID:12147696</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1la0" style="background-color:#fffaf0;"></div>

*[[Troponin|Troponin]]

[[Category: Chick]]

[[Category: Abusamhadneh, E M]]

[[Category: Dvoretsky, A]]

[[Category: Howarth, J W]]

[[Category: Rosevear, P R]]

[[Category: Troponin]]