Kinetic analysis of the interactions between Troponin C (TnC) and Troponin I (TnI) binding peptides: evidence for separate binding sites for the ?structural? N-terminus and the ?regulatory? C-terminus of TnI on TnC

2003 ◽  
Vol 16 (1) ◽  
pp. 37-53 ◽  
Author(s):  
Brian Tripet ◽  
Gregory De Crescenzo ◽  
Suzanne Grothe ◽  
Maureen O'Connor-McCourt ◽  
Robert S. Hodges
Keyword(s):  
Kinetic Analysis ◽  
Binding Sites ◽  
Troponin I ◽  
Troponin C ◽  
C Terminus ◽  
N Terminus ◽  
Binding Peptides

scholarly journals Proteolytic fragments of troponin C. Localization of high and low affinity Ca2+ binding sites and interactions with troponin I and troponin T

1978 ◽  
Vol 253 (15) ◽  
pp. 5452-5459
Author(s):  
P.C. Leavis ◽  
S.S. Rosenfeld ◽  
J. Gergely ◽  
Z. Grabarek ◽  
W. Drabikowski
Keyword(s):  
Binding Sites ◽  
Troponin I ◽  
Troponin T ◽  
Troponin C

scholarly journals Calcium- and Magnesium-Dependent Interactions between the C-Terminus of Troponin I and the N-Terminal, Regulatory Domain of Troponin C

2001 ◽  
Vol 387 (2) ◽  
pp. 243-249 ◽  
Author(s):  
Jeanne Digel ◽  
Omoefe Abugo ◽  
Tomoyoshi Kobayashi ◽  
Zygmunt Gryczynski ◽  
Joseph R. Lakowicz ◽  
...  
Keyword(s):  
Troponin I ◽  
Troponin C ◽  
Regulatory Domain ◽  
C Terminus ◽  
Calcium And Magnesium

Molecular Modeling and Virtual Screening of Molecular Inhibitors for Leptospiral Collagenase

2021 ◽  
Author(s):  
Vikram Kumar ◽  
Nagesh Srikaku ◽  
Veeranarayanan Surya Aathmanathan ◽  
Padikara K Satheeshkumar ◽  
Madanan Gopalakrishnan Madathiparambil ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Molecular Modeling ◽  
Active Site ◽  
Binding Sites ◽  
Catalytic Site ◽  
Simulation Studies ◽  
C Terminus ◽  
Ligand Binding Sites ◽  
N Terminus ◽  
The Stability

Abstract Collagenase is a virulence factor which facilitates the invasion of pathogenic Leptospira into the host. In the present study, the model of Leptopsiral collagenase was constructed by employing threading method with the crystal structure of collagenase G. Three ligand binding sites at N- terminus, catalytic site and C-terminus were predicted by Metapocket server. Among sixty seven inhibitors from the ChEBI and Zinc databases, Protohypericin is predicted as the best inhibitor since it binds at the catalytic site of Leptopsiral collagenase. Molecular dynamic simulation studies validated the stability of interaction between the active site of Leptospiral collagenase and Protohypericin. The docking and molecular simulation studies corroborated the potential of the ligand to curb leptospiral infection.

The binding sites of rabbit skeletal troponin-I on troponin-T

1980 ◽  
Vol 58 (8) ◽  
pp. 649-654 ◽  
Author(s):  
Joyce R. Pearlstone ◽  
Lawrence B. Smillie
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Site ◽  
Binding Sites ◽  
Troponin I ◽  
Troponin T ◽  
Gel Filtration ◽  
Troponin C ◽  
Separate Site

Various fragments derived from rabbit skeletal muscle troponin-T (Tn-T) by chemical and (or) proteolytic cleavage were mixed with whole troponin-I (Tn-I) and applied to a Sephadex G-75 gel filtration column in order to determine the binding site of Tn-I on Tn-T. This site of interaction was found to span two distinct regions of Tn-T. The first site involves the highly acidic NH2-terminal fragment CB3 (residues 1–70 of Tn-T). A second separate site is located in the region of residues 152–209 of Tn-T. The present study, in conjunction with our earlier work on tropomyosin – Tn-T binding and Tn-T – troponin-C binding, depicts Tn-T as being a functionally efficient molecule composed of several distinct domains of specialized amino acid sequence, each of which carries out a role in the binding of a different protein.

scholarly journals Biological activities of bovine cardiac-muscle troponin C C-terminal peptide (residues 84-161)

1982 ◽  
Vol 207 (2) ◽  
pp. 185-192 ◽  
Author(s):  
N V Barskaya ◽  
N B Gusev
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Cardiac Muscle ◽  
Sodium Dodecyl Sulphate ◽  
Binding Sites ◽  
Binding Constant ◽  
Troponin I ◽  
Biological Activities ◽  
Sodium Dodecyl ◽  
Troponin C

1. Bovine cardiac-muscle troponin C was digested at cysteine residues 35 and 84, and the C-terminal peptide (residues 84-161) was isolated. 2. The C-terminal peptide contains two Ca2+-binding sites. These sites bind Ca2+ with a binding constant of 2.0×10(8) M-1. In the presence of 2 mM-Mg2+ the binding constant for Ca2+ is decreased to 3.70×10(7) M-1. The corresponding constants for native troponin C are 5.90×10(7) M-1. and 2.90×10(7) M-1 respectively. 3. Electrophoretic mobility of the C-terminal peptide is increased in the presence of 0.1 mM-CaCl2 as compared with the mobility in the presence of 2mM-EDTA. The same phenomenon was observed when electrophoresis was performed in the presence of 6 M-urea or 0.1% sodium dodecyl sulphate. 4. When saturated with Ca2+, the C-terminal peptide forms complexes with bovine cardiac-muscle troponin I both in the absence and in the presence of 6 M-urea. This complex is dissociated on removal of Ca2+. 5. The data suggest that the C-terminal peptide of troponin C contains two Ca2+/Mg2+-binding sites and interacts with troponin I. Thus, despite the 30% difference in amino acid composition, the properties of bovine cardiac-muscle troponin C C-terminal peptide are similar to those of rabbit skeletal-muscle troponin C C-terminal peptide.

scholarly journals Recruitment of the inhibitor Cand1 to the cullin substrate adaptor site mediates interaction to the neddylation site

2011 ◽  
Vol 22 (1) ◽  
pp. 153-164 ◽  
Author(s):  
Kerstin Helmstaedt ◽  
Elke U. Schwier ◽  
Martin Christmann ◽  
Krystyna Nahlik ◽  
Mieke Westermann ◽  
...  
Keyword(s):  
Binding Site ◽  
Secondary Metabolism ◽  
Aspergillus Nidulans ◽  
Binding Sites ◽  
Ubiquitin Ligases ◽  
Cop9 Signalosome ◽  
C Terminus ◽  
N Terminus

Cand1 inhibits cullin RING ubiquitin ligases by binding unneddylated cullins. The Cand1 N-terminus blocks the cullin neddylation site, whereas the C-terminus inhibits cullin adaptor interaction. These Cand1 binding sites can be separated into two functional polypeptides which bind sequentially. C-terminal Cand1 can directly bind to unneddylated cullins in the nucleus without blocking the neddylation site. The smaller N-terminal Cand1 cannot bind to the cullin neddylation region without C-terminal Cand1. The separation of a single cand1 into two independent genes represents the in vivo situation of the fungus Aspergillus nidulans, where C-terminal Cand1 recruits smaller N-terminal Cand1 in the cytoplasm. Either deletion results in an identical developmental and secondary metabolism phenotype in fungi, which resembles csn mutants deficient in the COP9 signalosome (CSN) deneddylase. We propose a two-step Cand1 binding to unneddylated cullins which initiates at the adaptor binding site and subsequently blocks the neddylation site after CSN has left.

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