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Amazing Stability of the Arginine−Phosphate Electrostatic Interaction

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National Institute on Drug Abuse, Intramural Research Program, NIH, Department of Health and Human Services, Baltimore, Maryland 21224
Cite this: J. Proteome Res. 2005, 4, 4, 1397–1402
Publication Date (Web):July 6, 2005
Copyright © 2005 American Chemical Society

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    Abstract Image

    Electrostatic interactions between a basic epitope containing adjacent arginine residues and an acidic epitope containing a phosphorylated serine are involved in receptor heteromerization. In the present study, we demonstrate that this arginine−phosphate electrostatic interaction possesses a “covalent-like” stability. Hence, these bonds can withstand fragmentation by mass spectrometric collision-induced dissociation at energies similar to those that fragment covalent bonds and they demonstrate an extremely low dissociation constant by plasmon resonance. The present work also highlights the importance of phosphorylation−dephosphorylation events in the modulation of this electrostatic attraction. Phosphorylation of the acidic epitope, a casein kinase one consensus site, makes it available to interact with the basic epitope. On the other hand, phosphorylation of serine and/or threonine residues adjacent to the basic epitope, a protein kinase A consensus site, slows down the attraction between the epitopes. Although analyzed here in the frame of receptor heteromerization, the arginine-phosphate electrostatic interaction most likely represents a general mechanism in protein−protein interactions.

    Keywords: electrostatic interaction • receptor heteromers • phosphorylation • CK1 • PKA

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     To whom correspondence should be addressed. Amina S. Woods, NIDA IRP, NIH, 5500 Nathan Shock Drive, Baltimore, MD 21224. Tel:  410-550-1507. E-mail:  [email protected].

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