Molecular Recognition of Rhodopsin Kinase GRK1 and Recoverin Is Tuned by Switching Intra- and Intermolecular Electrostatic Interactions

Biochemistry ◽  
2019 ◽  
Vol 58 (43) ◽  
pp. 4374-4385 ◽  
Author(s):  
Seher Abbas ◽  
Valerio Marino ◽  
Daniele Dell’Orco ◽  
Karl-Wilhelm Koch
Keyword(s):  
Molecular Recognition ◽  
Electrostatic Interactions ◽  
Rhodopsin Kinase

scholarly journals Unexpected Specificity within Dynamic Transcriptional Protein-Protein Complexes

2020 ◽  
Author(s):  
Matthew J. Henley ◽  
Brian M. Linhares ◽  
Brittany S. Morgan ◽  
Tomasz Cierpicki ◽  
Carol A. Fierke ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Electrostatic Interactions ◽  
Protein Complexes ◽  
Critical Role ◽  
Gene Activation ◽  
Disordered Proteins ◽  
Conformational Ensemble ◽  
Regulation Of Transcription ◽  
Protein Protein Interaction ◽  
Eukaryotic Gene

AbstractA key functional event in eukaryotic gene activation is the formation of dynamic protein-protein interaction networks between transcriptional activators and transcriptional coactivators. Seemingly incongruent with the tight regulation of transcription, many biochemical and biophysical studies suggest that activators use nonspecific hydrophobic and/or electrostatic interactions to bind to coactivators, with few if any specific contacts. Here a mechanistic dissection of a set of representative dynamic activator•coactivator complexes, comprised of the ETV/PEA3 family of activators and the coactivator Med25, reveals a different molecular recognition model. The data demonstrate that small sequence variations within an activator family significantly redistribute the conformational ensemble of the complex while not affecting overall affinity, and distal residues within the activator—not often considered as contributing to binding—play a key role in mediating conformational redistribution. The ETV/PEA3•Med25 ensembles are directed by specific contacts between the disordered activator and the Med25 interface, which is facilitated by structural shifts of the coactivator binding surface. Taken together, these data highlight the critical role coactivator plasticity plays in recognition of disordered activators, and indicates that molecular recognition models of disordered proteins must consider the ability of the binding partners to mediate specificity.

scholarly journals Structural aspects of molecular recognition in the immune system. Part I: Acquired immunity (IUPAC Technical Report)

2014 ◽  
Vol 86 (10) ◽  
pp. 1435-1481 ◽  
Author(s):  
Douglas M. Templeton ◽  
Kerstin Moehle
Keyword(s):  
Molecular Recognition ◽  
Humoral Immunity ◽  
Influenza A ◽  
Electrostatic Interactions ◽  
Recent Literature ◽  
Process Variations ◽  
The Body ◽  
Soluble Antigen ◽  
Viral Antigens ◽  
Surface Shaping

Abstract Humoral immunity allows the body to mount a defense against pathogens and foreign substances, and to respond with memory to subsequent exposures. The molecular participants may also recognize self-structures, leading to attack on the body and autoimmune disease. The main players in humoral immunity are antibody-producing B lymphocytes, and several classes of T lymphocytes. This review deals with the molecular details of recognition of antigens by soluble antibodies, and of substances presented to receptors on the surfaces of T cells (TCRs). The prototype antibody consists of a dimer of dimers, two heavy (H) chains and two light (L) chains, with antigen recognition capacity lying in variable “head” regions of an H-L pair. Most crystallographic studies are done with this substructure, called a Fab fragment, bound in a soluble antigen complex. Homologous to this arrangement, the prototype TCR consists of two chains (α and β) that complex not soluble antigen, but usually a short peptide or other small molecule presented by proteins of the major histocompatibility complex. In each case a general background on the historical development of understanding the molecular recognition interface is given, followed by a number of examples of crystal structures from the recent literature that have allowed us to refine our understanding of the complex recognition process. Variations on the prototypical structures are also considered. The spectrum of recognition strategies involves interplay of lock-and-key with flexibility, varying degrees of entropic and enthalpic contributions, surface shaping by entrapped water molecules, and combinations of stabilizing hydrogen bonding, electrostatic interactions, salt bridging, and van der Waals forces. Preeminent in the recent literature are details of antibody binding to influenza A and human immunodeficiency viral antigens. Both viral antigens and attempts to understand autoimmunity are prominent in the recent TCR literature.

scholarly journals Molecular Recognition by Pillar[5]arenes: Evidence for Simultaneous Electrostatic and Hydrophobic Interactions

Pharmaceutics ◽  
2021 ◽  
Vol 14 (1) ◽  
pp. 60
Author(s):  
Borja Gómez-González ◽  
Luis García-Río ◽  
Nuno Basílio ◽  
Juan C. Mejuto ◽  
Jesus Simal-Gandara
Keyword(s):  
Molecular Recognition ◽  
Inclusion Complexes ◽  
Electrostatic Interactions ◽  
Alkyl Chain ◽  
Hydrophobic Interactions ◽  
Binding Constants ◽  
Ionic Interactions ◽  
Hydrophobic Effects ◽  
Hydrophobic Character ◽  
Electrostatic And Hydrophobic Interactions

The formation of inclusion complexes between alkylsulfonate guests and a cationic pillar[5]arene receptor in water was investigated by NMR and ITC techniques. The results show the formation of host-guest complexes stabilized by electrostatic interactions and hydrophobic effects with binding constants of up to 107 M−1 for the guest with higher hydrophobic character. Structurally, the alkyl chain of the guest is included in the hydrophobic aromatic cavity of the macrocycle while the sulfonate groups are held in the multicationic portal by ionic interactions.

scholarly journals 1L1415 Effects of ligand-receptor electrostatic interactions on molecular recognition of glutamate receptor

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S70
Author(s):  
M. Kubo ◽  
E. Shiomitsu ◽  
K. Odai ◽  
T. Sugimoto ◽  
H. Suzuki ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Glutamate Receptor ◽  
Electrostatic Interactions

scholarly journals An intrinsic compartmentalization code for peripheral membrane proteins in photoreceptor neurons

2019 ◽  
Vol 218 (11) ◽  
pp. 3753-3772 ◽  
Author(s):  
Nycole A. Maza ◽  
William E. Schiesser ◽  
Peter D. Calvert
Keyword(s):  
Membrane Proteins ◽  
Protein Interactions ◽  
Electrostatic Interactions ◽  
Transport Model ◽  
Fluorescent Proteins ◽  
Lipid Binding ◽  
Peripheral Membrane Proteins ◽  
Rhodopsin Kinase ◽  
Membrane Bound ◽  
Photoreceptor Neurons

In neurons, peripheral membrane proteins are enriched in subcellular compartments, where they play key roles, including transducing and transmitting information. However, little is known about the mechanisms underlying their compartmentalization. To explore the roles of hydrophobic and electrostatic interactions, we engineered probes consisting of lipidation motifs attached to fluorescent proteins by variously charged linkers and expressed them in Xenopus rod photoreceptors. Quantitative live cell imaging showed dramatic differences in distributions and dynamics of the probes, including presynapse and ciliary OS enrichment, depending on lipid moiety and protein surface charge. Opposing extant models of ciliary enrichment, most probes were weakly membrane bound and diffused through the connecting cilium without lipid binding chaperone protein interactions. A diffusion-binding-transport model showed that ciliary enrichment of a rhodopsin kinase probe occurs via recycling as it perpetually leaks out of the ciliary OS. The model accounts for weak membrane binding of peripheral membrane proteins and a leaky connecting cilium diffusion barrier.

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