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The FHA domain is linked to the kinase/phosphatase catalytic domain by a flexible tether, and it exhibits a mode of target selection based on electrostatic complementarity between the binding surface and the phosphothreonine peptide.
Consequently, there exist an electrostatic complementarity between the target protein and the designed peptide.
Collectively, the Cre, Flp and topoisomerase results highlight the contribution of conserved electrostatic complementarity between substrate and active site towards transition state stabilization during site-specific recombination and DNA relaxation.
The Syndapin EFC domain associates significantly more strongly (KD 88 nM) than epsin 1 due to the large electrostatic complementarity between the basic concave surface and the negatively charged convex liposome surface.
Authors' response (17): We have expanded and modified Fig. 4 to show the electrostatic complementarity between the interacting surfaces of cytochrome c and Apaf-1.
While the structural and dynamics differences between PYDs are more numerous than the similarities, work on the signaling adaptor protein ASC and its inhibitor ASC2 showed the importance of electrostatic complementarity between PYD domains for their interactions.
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Both global shape and electrostatic complementarities between the Nb epitope-recognition sites and the GAK antigens provide a structural basis for selection of the binding site (details in Supplementary Figures S3A and S3C at http://www.biochemj.org/bj/459/bj4590059add.htm).htm
The SH3 rotation results in a polar interface between SH3 and PH-TH, with good electrostatic complementarity, which preserves the interactions between the SH3 domain, the linker and the N lobe of the kinase.
A remarkable feature at the interface of the complex is the electrostatic complementarity observed surrounding the aromatic stacking interaction between Trp89A-Phe29B, in which the Phe29B belonging to CCL3 is buried in a negatively charged pocket due to the presence of Glu30B and to the proximity of Asp6B from CCL3 N-terminal region.
This finding is consistent, albeit not confirmatory, of a transient and direct physical interaction between the cognate chaperone and the "throat" of the pump via electrostatic complementarity.
Analysis of the putative interactions between AcpS and ACPM from Mtb, based on a comparison with the complex structure from Bacillus subtilis, showed that the Mtb AcpS and ACPM lack the electrostatic complementarity observed in B. subtilis.
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