J. Maharana

Structure of the human Duffy antigen receptor

This study determines the cryo-EM structure of the Duffy antigen receptor bound to CCL7, revealing structural features that explain its unique functional properties and lack of G protein coupling.

Molecular insights into atypical modes of beta-arrestin interaction with seven transmembrane receptors

This study presents cryo-EM structures and experimental data revealing how beta-arrestins interact with GPCRs, particularly those with phosphorylation in the third intracellular loop and intrinsically biased receptors.

Structure-guided engineering of biased-agonism in the human niacin receptor via single amino acid substitution

This study presents cryo-EM structures of GPR109A-G-protein complexes with agonists and uses them to engineer biased agonists with reduced flushing effects.

Structural insights into agonist-binding and activation of the human complement C3a receptor

This study presents structural insights into C3a-C3aR interactions and identifies a G-protein-biased agonist for the receptor.

Structural insights into ligand-recognition, activation, and signaling-bias at the complement C5a receptor, C5aR1

This study presents cryo-EM structures of C5aR1 bound to C5a and a synthetic peptide, revealing conformational changes and G-protein coupling mechanisms.

Structural snapshots uncover a lock-and-key type conserved activation mechanism of β-arrestins by GPCRs

The paper presents structural snapshots of β-arrestins interacting with GPCRs, revealing a conserved 'lock-and-key' activation mechanism through specific phosphorylation patterns.

Molecular insights into intrinsic transducer-coupling bias in the CXCR4-CXCR7 system

This study characterizes the biased agonism of CXCR4 and CXCR7, revealing differences in G-protein coupling, β-arrestin recruitment, and ERK1/2 activation.

Allosteric modulation of GPCR-induced β-arrestin trafficking and signaling by a synthetic intrabody

This paper shows that a synthetic intrabody enhances β-arrestin endosomal trafficking and ERK1/2 activation in a GPCR mutant by promoting an active-like conformation.

Crystal structure of β-arrestin 2 in complex with an atypical chemokine receptor phosphopeptide reveals an alternative active conformation

The paper presents a crystal structure of β-arrestin 2 bound to a phosphopeptide from ACKR3, revealing an alternative active conformation distinct from β-arrestin 1.

Conformational sensors and domain-swapping reveal structural and functional differences between β-arrestin isoforms

The paper identifies structural differences between β-arrestin isoforms using conformational sensors and domain-swapping, linking these differences to their distinct functional outcomes in GPCR signaling.