Ali Khalid Khan, MD, PhD
Clinical FellowAbout
Research
Publications
2021
Cryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs
Khan A, Jagielnicki M, Bennett B, Purdy M, Yeager M. Cryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs. Structure 2021, 29: 1040-1047.e3. PMID: 34129834, PMCID: PMC9616683, DOI: 10.1016/j.str.2021.05.010.Peer-Reviewed Original ResearchConceptsLipid bilayer nanodiscsGap junction channelsHexameric hemichannelsExtracellular loopBilayer nanodiscsTransmembrane α-helicesCryo-EM structureGap junction hemichannelsAdjacent cell membranesIntercellular conduitsCell communicationCx hemichannelsPlasma membraneOpen conformationSecond extracellular loopJunction channelsΑ-helixConformational flexibilityCell membraneHemichannelsCx isoformsExtracellular spaceNanodiscsStructural foundationMembrane
2020
A Steric “Ball-and-Chain” Mechanism for pH-Mediated Regulation of Gap Junction Channels
Khan A, Jagielnicki M, McIntire W, Purdy M, Dharmarajan V, Griffin P, Yeager M. A Steric “Ball-and-Chain” Mechanism for pH-Mediated Regulation of Gap Junction Channels. Cell Reports 2020, 31: 107482. PMID: 32320665, PMCID: PMC10290761, DOI: 10.1016/j.celrep.2020.03.046.Peer-Reviewed Original Research
2018
PH-Gating of GAP Junction Channels: Visualization of a “Ball-and-Chain” by Cryo-EM
Khan A, Jagielnicki M, Purdy M, Yeager M. PH-Gating of GAP Junction Channels: Visualization of a “Ball-and-Chain” by Cryo-EM. Biophysical Journal 2018, 114: 162a. DOI: 10.1016/j.bpj.2017.11.904.Peer-Reviewed Original Research
2014
Function and dynamics of macromolecular complexes explored by integrative structural and computational biology
Purdy M, Bennett B, McIntire W, Khan A, Kasson P, Yeager M. Function and dynamics of macromolecular complexes explored by integrative structural and computational biology. Current Opinion In Structural Biology 2014, 27: 138-148. PMID: 25238653, PMCID: PMC6387792, DOI: 10.1016/j.sbi.2014.08.006.Peer-Reviewed Original ResearchConceptsMacromolecular complexesX-ray crystallographyIntegrative structural biologyG protein complexProtein complexesStructural biologyMD simulationsMicrosecond MD simulationsFunctional dynamicsX-ray crystallographic dataMolecular dynamics simulationsComputational biologyBiologyNew insightsBiological systemsCrystallographic dataUnprecedented synergyDynamics simulationsCrystallographyComplexesFunctional propertiesRibosomesTransmembraneGPCRsAdrenergic receptors
2013
Controlled drug-release system based on pH-sensitive chloride-triggerable liposomes
Wehunt MP, Winschel CA, Khan AK, Guo TL, Abdrakhmanova GR, Sidorov V. Controlled drug-release system based on pH-sensitive chloride-triggerable liposomes. Journal Of Liposome Research 2013, 23: 37-46. PMID: 23363303, DOI: 10.3109/08982104.2012.727423.Peer-Reviewed Original Research
2012
Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions.
Mokdad A, Herrick DZ, Kahn AK, Andrews E, Kim M, Cafiso DS. Ligand-induced structural changes in the Escherichia coli ferric citrate transporter reveal modes for regulating protein-protein interactions. Journal Of Molecular Biology 2012, 423: 818-30. PMID: 22982293, PMCID: PMC3472153, DOI: 10.1016/j.jmb.2012.09.003.Peer-Reviewed Original Research
2011
Molecular Origin of Electron Paramagnetic Resonance Line Shapes on β-Barrel Membrane Proteins: The Local Solvation Environment Modulates Spin-Label Configuration
Freed D, Khan A, Horanyi P, Cafiso D. Molecular Origin of Electron Paramagnetic Resonance Line Shapes on β-Barrel Membrane Proteins: The Local Solvation Environment Modulates Spin-Label Configuration. Biochemistry 2011, 50: 8792-8803. PMID: 21894979, PMCID: PMC3199607, DOI: 10.1021/bi200971x.Peer-Reviewed Original ResearchMeSH KeywordsBacterial Outer Membrane ProteinsBinding SitesCrystallography, X-RayElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsLipid BilayersMembrane ProteinsMembrane Transport ProteinsModels, MolecularMutagenesisProtein ConformationProtein Structure, SecondaryProtein Structure, TertiarySolventsSpin LabelsConceptsLine shapeLong-range distance restraintsEPR spectraResonance line shapeΒ-barrel membrane proteinsDifferent rotameric statesFast rotationRotameric statesElectron paramagnetic resonance spectroscopyEPR line shapeParamagnetic resonance spectroscopyMulticomponent spectraElectron paramagnetic resonance line shapesSpectraWeak interactionsProtein-lipid interfaceAtomic resolution structuresDistance restraintsBilayer thicknessLipid environmentLipid bilayersStructure refinementMembrane-facing surfaceProtein structure refinementResonance spectroscopyMolecular Basis of Transmembrane Signaling in a Membrane Transporter
Freed D, Yen C, Khan A, Horanyi P, Wiener M, Cafiso D. Molecular Basis of Transmembrane Signaling in a Membrane Transporter. Biophysical Journal 2011, 100: 243a. DOI: 10.1016/j.bpj.2010.12.1545.Peer-Reviewed Original Research
2009
ChemInform Abstract: One‐Pot Tandem Decarboxylative Allylation—Heck Cyclization of Allyl Diphenylglycinate Imines: Rapid Access to Polyfunctionalized 1‐Aminoindans.
Fields W, Khan A, Sabat M, Chruma J. ChemInform Abstract: One‐Pot Tandem Decarboxylative Allylation—Heck Cyclization of Allyl Diphenylglycinate Imines: Rapid Access to Polyfunctionalized 1‐Aminoindans. ChemInform 2009, 40: no-no. DOI: 10.1002/chin.200915093.Peer-Reviewed Original Research
2008
One-Pot Tandem Decarboxylative Allylation−Heck Cyclization of Allyl Diphenylglycinate Imines: Rapid Access to Polyfunctionalized 1-Aminoindanes
Fields W, Khan A, Sabat M, Chruma J. One-Pot Tandem Decarboxylative Allylation−Heck Cyclization of Allyl Diphenylglycinate Imines: Rapid Access to Polyfunctionalized 1-Aminoindanes. Organic Letters 2008, 10: 5131-5134. PMID: 18956870, DOI: 10.1021/ol801986m.Peer-Reviewed Original Research