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clustalw multiple alignment algorithm  (MacVector inc)

 
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    Structured Review

    MacVector inc clustalw multiple alignment algorithm
    Cardiac TnT contains a highly conserved PKA docking site. A, schematic illustration shows the location of the PKA binding site and cardiac-specific cTnI-Ser23-Ser24 phosphorylation sites (star). Drawing of the troponin complex is based on the crystal structure of the troponin core domain (50). N-terminal region of cTnT (residues 1–204) was not solved in the crystal structure. Rectangles represent helical structures. cTnC is colored red, cTnI is green, and cTnT is blue. B, <t>ClustalW</t> multiple sequence alignment of cTnT with nine other AKAPs. Conserved residues responsible for tethering PKA are shown in white. The high homology between cTnT and Ht31 is also shown (boxed). C, surface representation of cTnT (PDB 1J1D) helix 203–224 shows the position of hydrophobic residues (red) involved in PKA docking.
    Clustalw Multiple Alignment Algorithm, supplied by MacVector inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/clustalx+multiple-sequence+alignment+program/pmc03013013-417-11-18?v=MacVector+inc
    Average 90 stars, based on 1 article reviews
    clustalw multiple alignment algorithm - by Bioz Stars, 2026-08
    90/100 stars

    Images

    1) Product Images from "Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments * "

    Article Title: Cardiac Troponin T, a Sarcomeric AKAP, Tethers Protein Kinase A at the Myofilaments *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.148684

    Cardiac TnT contains a highly conserved PKA docking site. A, schematic illustration shows the location of the PKA binding site and cardiac-specific cTnI-Ser23-Ser24 phosphorylation sites (star). Drawing of the troponin complex is based on the crystal structure of the troponin core domain (50). N-terminal region of cTnT (residues 1–204) was not solved in the crystal structure. Rectangles represent helical structures. cTnC is colored red, cTnI is green, and cTnT is blue. B, ClustalW multiple sequence alignment of cTnT with nine other AKAPs. Conserved residues responsible for tethering PKA are shown in white. The high homology between cTnT and Ht31 is also shown (boxed). C, surface representation of cTnT (PDB 1J1D) helix 203–224 shows the position of hydrophobic residues (red) involved in PKA docking.
    Figure Legend Snippet: Cardiac TnT contains a highly conserved PKA docking site. A, schematic illustration shows the location of the PKA binding site and cardiac-specific cTnI-Ser23-Ser24 phosphorylation sites (star). Drawing of the troponin complex is based on the crystal structure of the troponin core domain (50). N-terminal region of cTnT (residues 1–204) was not solved in the crystal structure. Rectangles represent helical structures. cTnC is colored red, cTnI is green, and cTnT is blue. B, ClustalW multiple sequence alignment of cTnT with nine other AKAPs. Conserved residues responsible for tethering PKA are shown in white. The high homology between cTnT and Ht31 is also shown (boxed). C, surface representation of cTnT (PDB 1J1D) helix 203–224 shows the position of hydrophobic residues (red) involved in PKA docking.

    Techniques Used: Binding Assay, Phospho-proteomics, Sequencing



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