TY - JOUR
T1 - Interaction of troponin I and troponin C
T2 - use of the two-dimensional transferred nuclear Overhauser effect to determine the structure of a Gly-110 inhibitory troponin I peptide analog when bound to cardiac troponin C
AU - Campbell, A. Patricia
AU - Van Eyk, Jennifer E.
AU - Hodges, Robert S.
AU - Sykes, Brian D.
N1 - Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.
PY - 1992/11/10
Y1 - 1992/11/10
N2 - The structure of a peptide analog of the inhibitory region of cardiac troponin-1 (N-acetyl-G110-TnI(104-115)amide) when bound to cardiac troponin-C has been determined by 2-dimensional 1H-NMR techniques. The bound structure determined for this peptide is similar to that determined previously for the skeletal peptide (which has a proline at position 110) bound to skeletal troponin-C (Campbell and Sykes (1991) J. Mol. Biol. 222, 405-412). This structure shows a helical like peptide backbone "bent" around P109-G110 to bring the hydrophobic residues F1106, L111 and V114 closer together. The other "side" of this structure is surrounded by the basic residues extending outwards towards the protein or solution. While the bound structures of the cardiac and skeletal peptides are shown to be quite similar, the cardiac peptide appears more flexible near the central glycine residue.
AB - The structure of a peptide analog of the inhibitory region of cardiac troponin-1 (N-acetyl-G110-TnI(104-115)amide) when bound to cardiac troponin-C has been determined by 2-dimensional 1H-NMR techniques. The bound structure determined for this peptide is similar to that determined previously for the skeletal peptide (which has a proline at position 110) bound to skeletal troponin-C (Campbell and Sykes (1991) J. Mol. Biol. 222, 405-412). This structure shows a helical like peptide backbone "bent" around P109-G110 to bring the hydrophobic residues F1106, L111 and V114 closer together. The other "side" of this structure is surrounded by the basic residues extending outwards towards the protein or solution. While the bound structures of the cardiac and skeletal peptides are shown to be quite similar, the cardiac peptide appears more flexible near the central glycine residue.
KW - (Heart)
KW - Nuclear Overhauser effect
KW - Troponin
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U2 - 10.1016/0167-4838(92)90036-D
DO - 10.1016/0167-4838(92)90036-D
M3 - Article
C2 - 1420332
AN - SCOPUS:0026470719
VL - 1160
SP - 35
EP - 54
JO - BBA - Protein Structure
JF - BBA - Protein Structure
SN - 1570-9639
IS - 1
ER -