Results: 3

1.
Figure 2

Figure 2. Sequence conservation. From: Molecular and Functional Characterization of Novel Hypertrophic Cardiomyopathy Susceptibility Mutations in TNNC1- Encoded Troponin C.

The identified mutations in TNNC1 localize to residues completely conserved across all species queried.

Andrew P. Landstrom, et al. J Mol Cell Cardiol. ;45(2):281-288.
2.
Figure 3

Figure 3. The Ca2+ dependence of force development and maximal relative force in reconstituted muscle fibers. From: Molecular and Functional Characterization of Novel Hypertrophic Cardiomyopathy Susceptibility Mutations in TNNC1- Encoded Troponin C.

A) Ca2+ dependence of force development in (●) WT, (▲) A8V, (♦) C84Y, (▼) E134D, and (■) D145E. B) Relative force recovery measured after HcTnC reconstitution normalized to the initial force. Data in each experiment are the average of 7–9 experiments and are expressed as mean ± S.E. in Table 3.

Andrew P. Landstrom, et al. J Mol Cell Cardiol. ;45(2):281-288.
3.
Figure 1

Figure 1. Mapping and modeling of HCM-susceptibility mutations in TNNC1-encoded cardiac troponin C (HcTnC). From: Molecular and Functional Characterization of Novel Hypertrophic Cardiomyopathy Susceptibility Mutations in TNNC1- Encoded Troponin C.

A) The gene and protein linear topology of HcTnC, including exon, splice junction, functional domains, and calcium binding site locations. The location of each of the four mutations is noted respectively. B) N-terminus (left) depicting the location of A8V and C84Y mutations in relationship to the Ca2+ binding sites and HcTnC helices. Ca2+ binding site I is defunct and Ca2+ binding site II shows Ca2+ bound (green sphere); N-helix (blue), A-helix (pink), B-helix (green), C-helix (orange), and D-helix (red). The Ala8 is located in the first helix of TnC in the beginning of the flexible linker connecting the two domains. C-terminus (right) depicting the location of E134D and D145E mutations in relationship to Ca2+ binding sites and helices. Ca2+ binding site III and IV pictured with Ca2+ bound (green spheres); E-helix (blue), F-helix (pink), G-helix (orange), H-helix (red). Glu134 is located in the G-helix between Ca2+ binding sites III and IV and Asp145 is situated at the Z position of Ca2+ coordinating residues of site IV.

Andrew P. Landstrom, et al. J Mol Cell Cardiol. ;45(2):281-288.

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