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.

bioRxiv · Jul 9, 2023 · PreprintBiochemistry

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

J. Maharana, F. K. Sano, P. Sarma, M. K. Yadav, L. Duan, T. M. Stepniewski, M. Chaturvedi, A. Ranjan, V. Singh, S. Saha, G. Mahajan, M. Chami, W. Shihoya, J. Selent, K. Y. Chung, , A. K. Shukla

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.

bioRxiv · Jul 5, 2023Biochemistry

A dissemination-prone morphotype enhances extrapulmonary organ entry by the fungus Cryptococcus neoformans

S. T. Denham, B. Brammer, K. Y. Chung, M. A. Wambaugh, J. Bednarek, L. Guo, J. C. S. Brown

This study shows that a small morphotype of Cryptococcus neoformans, called 'seed' cells, is critical for extrapulmonary organ entry and is induced by environmental factors like phosphate.

bioRxiv · Aug 27, 2020Microbiology

Integrative modelling of the full-length human dehydrodolichyl diphosphate synthase using a hybrid computational and experimental approach

M. Lisnyansky Barel, S. Y. Lee, A. Y. Ki, N. Kapelushnik, A. Loewenstein, K. Y. Chung, D. Schneidman-Duhovny, M. Giladi, H. Newman, Y. Haitin

The paper presents a structural model of full-length human DHDDS using computational and experimental methods, revealing a helix-loop-helix motif in the C-terminal domain and a DHDDS-NgBR heterodimer structure.

bioRxiv · Oct 7, 2019Biophysics

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

K. Min, H.-J. Yoon, J. Y. Park, M. Baidya, H. Dwivedi, J. Maharana, K. Y. Chung, A. K. Shukla, H. H. Lee

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.

bioRxiv · Sep 29, 2019 · PreprintBiochemistry

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

E. Ghosh, H. Dwivedi, M. Baidya, A. Srivastava, P. Kumari, T. Stepniewski, H. R. Kim, M.-H. Lee, J. v. Gastel, M. Chaturvedi, D. Roy, S. Pandey, J. Maharana, R. Guixa-Gonzalez, L. M. Luttrell, , A. K. Shukla

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.

bioRxiv · Aug 5, 2019Biophysics