Author

B. Khanppnavar

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4 Biophysics· 2 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Assay:cryo-EM· 5 Research Focus:protein structure prediction· 5 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Organism:bacteria (other)· 1 Research Focus:drug response / drug discovery· 1 Approach:mechanistic / dynamical model· 1

Frequent Co-Authors

V. M. Korkhov· 5 shared D. Schuster· 3 shared P. Lavriha· 3 shared P. Picotti· 3 shared V. Mehta· 3 shared C. Qi· 2 shared A. Inoue· 1 shared A. K. Shukla· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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5 shared papersBiochemistry

V. M. Korkhov

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Author profile →

7 papers

Recent·Most cited

Structural basis of connexin-36 gap junction channel inhibition

X. Ding, S. Aureli, A. Vaithia, P. Lavriha, D. Schuster, B. Khanppnavar, X. Li, T. B. Blum, P. Picotti, F. L. Gervasio, V. M. Korkhov

The paper reports the cryo-EM structure of connexin-36 bound to mefloquine, revealing how small molecules inhibit gap junction channels by partially occluding the pore and altering electrostatics.

bioRxiv · Dec 9, 2023Biophysics

Structure of the human Duffy antigen receptor

S. Saha, B. Khanppnavar, J. Maharana, H. Kim, C. M. C. Carino, C. Daly, S. Houston, P. Kumari, P. N. Yadav, B. Plouffe, A. Inoue, K. Y. Chung, R. Banerjee, V. M. Korkhov, A. K. Shukla

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

Regulatory sites of CaM-sensitive adenylyl cyclase AC8 revealed by cryo-EM and structural proteomics

B. Khanppnavar, D. Schuster, P. Lavriha, F. Uliana, M. Özel, V. Mehta, A. Leitner, P. Picotti, V. M. Korkhov

The paper determines the cryo-EM structure of bovine AC8 bound to CaM and Gs, identifies interaction sites, and infers conformational changes in the regulation mechanism.

bioRxiv · Mar 3, 2023Biochemistry

Structural basis of organic cation transporter-3 inhibition

B. Khanppnavar, J. Maier, F. Herborg, R. Gradisch, E. Lazzarin, D. Luethi, J.-W. Yang, C. Qi, M. Holy, K. Jaentsch, O. Kudlacek, K. Schicker, T. Werge, U. Gether, T. Stockner, , H. H. Sitte

The paper determines the cryo-EM structure of OCT3 and analyzes genetic variants to understand its function and inhibition.

bioRxiv · Jul 14, 2022Pharmacology & Toxicology

Structure of Mycobacterium tuberculosis Cya, an evolutionary ancestor of the mammalian membrane adenylyl cyclases

V. Mehta, B. Khanppnavar, D. Schuster, I. Kantarci, I. Vercellino, A. Kosturanova, T. Iype, S. Stefanic, P. Picotti, V. M. Korkhov

The paper determines the cryo-EM structure of Mycobacterium tuberculosis Cya, revealing its TM domain's role in catalytic activity regulation.

bioRxiv · Dec 1, 2021Biochemistry

Structural basis of adenylyl cyclase 9 activation

C. Qi, P. Lavriha, V. Mehta, B. Khanppnavar, I. Mohammed, Y. Li, M. Lazaratos, J. V. Schaefer, B. Dreier, A. Plueckthun, A.-N. Bondar, C. W. Dessauer, V. M. Korkhov

The paper presents cryo-EM structures of AC9 in different states to reveal activator-induced conformational changes essential for its activation.

bioRxiv · Aug 11, 2021Biochemistry

Deciphering the structural intricacy in virulence effectors for proton-motive force mediated unfolding and type-III protein secretion

B. Khanppnavar, A. Roy, K. Chandra, N. C. Maiti, S. Datta

This study investigates how pathogenic bacteria use proton-motive force to unfold and secrete virulence effectors efficiently, revealing structural and energetic mechanisms involved.

bioRxiv · Feb 21, 2019Biophysics