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PEP-19 modulates calcium binding to calmodulin by electrostatic steering
Colowick; Editor-Nathan P. Kaplan; Editor-Anthony R. Means; Editor-P. Michael Conn.
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Structure and Regulation of Calcium/Calmodulin-Dependent Protein Kinases | Chemical Reviews
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The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since , each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike.
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The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences. Seller Inventory EOD More information about this seller Contact this seller About this Item:. Condition: Like New. Very light use, FINE or better, very minor shelf wear. For non-UK markets items of 1. Published by Oxford University Press About this Item: Oxford University Press, A Nature Research Journal. CaM consists of globular N- and C-domains connected by a flexible linker that allows structural diversity in target protein recognition 1 , 2 , 3.
Our search for such regulators of CaM signalling led us to a small, intrinsically disordered protein called PEP Although originally identified in the central nervous system 10 , PEP mRNA is also found in human bladder, kidney, prostate, uterus, thyroid, cardiac and adrenal tissues. For example, PEP null mice show a dramatic reduction in long-term plasticity at synapses between granule cell parallel fibres and Purkinje cells 11 , as well as altered cardiac excitability Overexpression of PEP in PC12 cells increases neurite outgrowth 13 , and premature neuronal differentiation is seen in transgenic mice with three copies of the PEP gene PEP has essentially no effect on backbone amide chemical shifts in the N-domain of apo CaM with an average change of only 0.
In contrast, the average chemical shift perturbation across residues 81— in the C-domain of CaM is 0. Supplementary Fig.
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Figure 1a shows that association with apo C-CaM has no effect on amide chemical shifts of residues 1—29 in 15 N-labelled PEP, but large changes are observed for residues 30—58, which span both the acidic sequence and core IQ motif see full spectra in Supplementary Fig. The open bar in Fig. Table 1 shows restraints used for structure calculations as well as structural statistics for an ensemble of the 20 lowest energy structures.
Cellular regulators part A : Calcium and calmodulin-binding proteins
Figure 2a shows a stereo view of the 20 lowest energy structures. Consistent with the data in Fig. Figure 2b shows the minimized average structure of the ensemble, excluding the disordered N-terminal region in PEP Apo C-CaM is shown in dark blue. The disordered N terminus aa 1—29 , acidic sequence aa 30—40 and IQ motif aa 41—62 are shown in gold, red and light blue, respectively. The colour scheme is the same as in a. All other figures also use the averaged minimized structure for the ensemble. Second, Supplementary Fig. This is consistent with amide line broadening observed for residues — due to chemical exchange, which was also seen for apo CaM bound to the IQ motif peptide of Na V 1.
Figure 3b shows that these residues red are predominantly located on one surface of the helical segment in PEP The importance of these residues for binding to CaM is supported by a study using synthetic peptides that span residues 36—60 in the IQ motif of PEP ref. This extensive network of NOEs is illustrated in Fig. This network of hydrophobic interactions may provide allosteric communication between the acidic loop and helical region of PEP bound to apo C-CaM. As mentioned above, the conformation of loop III is similar in both structures. Figure 4a shows that Pro37 terminates the helical segment of PEP, and intramolecular NOEs show that Pro37 and Ala36 interact with neighbouring residues to stabilize the transition between helical and coiled segments in PEP Thus, a plausible hypothesis is that conversion of Pro37 to Gly confers a high degree of flexibility that inhibits residues 30—36 from properly interacting with CaM.
To test this hypothesis, we used chemical shift perturbation mapping and paramagnetic relaxation enhancement PRE to determine the effects of mutation of Pro37 on the structure and position of the acidic sequence. In contrast, Supplementary Fig. In addition, Supplementary Fig. This is consistent with Supplementary Fig. The grey bars in Fig. A significant PRE effect is also seen for Gln and Val, which is consistent with the location of these two residues in a short beta strand in site IV that forms a beta sheet with residues in site III.
Calcium binding loop III is shown in yellow. The coloured vertical lines in Fig. A red line indicates that the distance between the corresponding backbone amide in C-CaM and the spin label bound to Cys31 is increased by mutation of Pro37 to Gly. Conversely, a blue line indicates a decreased distance.
sphereaudiosystems.com/1373-cocospy-redmi.php We report here the first structure of a complex between apo CaM and a protein that regulates the activity of CaM, instead of a target protein that is regulated by CaM. Figure 7 shows that the backbone oxygen and beta protons of Asp93 contribute to formation of the negatively charged basin. As illustrated by the green arrows in Fig. The surface contributed by Asp93 in C-CaM is shown as transparent, and is located in negatively charged basin. It is well established that electrostatic interactions can increase the rate of protein-protein and protein-ligand association by orders of magnitude 27 , This is consistent with Fig.
Mutation of Pro37 to Gly has the greatest effect on the ability of PEP because it destabilizes the interaction between the acidic sequence and site III of CaM, thereby affecting the relative position of multiple acidic residues. Finally, Martin et al. Arrowheads indicate the position of acidic residues in the acidic sequences of PEP and Ng. From a broader perspective, the high content of polar and charged residues in intrinsically disordered proteins makes them well suited to modulate ligand binding by changing the surface topology and electrostatic potential on binding to target proteins.