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Dr. Amir Khan

Associate Professor (Biochemistry)

 X-ray Crystallographic Studies of Poxvirus-Mediated Antagonism of TLR signaling

Mulvaney E.P, O'Meara F, Khan A.R, O'Connell D.J, Kinsella B.T, Identification of α-helix 4 (α4) of Rab11a as a novel Rab11-binding domain (RBD): Interaction of Rab11a with the Prostacyclin Receptor, Biochimica et Biophysica Acta - Molecular Cell Research, 1864, (10), 2017, p1819 - 1832, Journal Article, PUBLISHED  DOI  URL
Nounamo B, Li Y, O'Byrne P, Kearney A.M, Khan A, Liu J, An interaction domain in human SAMD9 is essential for myxoma virus host-range determinant M062 antagonism of host anti-viral function, Virology, 503, 2017, p94 - 102, Journal Article, PUBLISHED  DOI  URL
Oliveira T, Sharkey M.A, Engel P.C, Khan A.R, Crystal structure of a chimaeric bacterial glutamate dehydrogenase, Acta Crystallographica Section:F Structural Biology Communications, 72, 2016, p462 - 466, Notes: [Export Date: 22 September 2016], Journal Article, PUBLISHED  DOI  URL
Lall, P., Lindsay, A.J., Hanscom, S., (...), McCaffrey, M.W., Khan, A.R., Structure-function analyses of the interactions between Rab11 and Rab14 small GTPases with their shared effector Rab coupling protein (RCP), Journal of Biological Chemistry, 290, (30), 2015, 18817-18832 , Notes: [ ], Journal Article, PUBLISHED  TARA - Full Text  DOI
Franklin, E., Khan, A.R., Poxvirus antagonism of innate immunity by Bcl-2 fold proteins, Journal of Structural Biology, 181, (1), 2013, p1-10 , Notes: [ ], Journal Article, PUBLISHED  DOI
Lall, P., Horgan, C.P., Oda, S., (...), McCaffrey, M.W., Khan, A.R., Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase, Biochimica et Biophysica Acta - Proteins and Proteomics , 1834, (12), 2013, p2679-2690 , Journal Article, PUBLISHED  DOI
Sharkey MA, Oliveira TF, Engel PC, Khan AR, Structure of NADP(+)-dependent glutamate dehydrogenase from Escherichia coli--reflections on the basis of coenzyme specificity in the family of glutamate dehydrogenases., The FEBS journal, 280, (18), 2013, p4681-92 , Journal Article, PUBLISHED  DOI
Khan AR, Oligomerization of rab/effector complexes in the regulation of vesicle trafficking., Progress in molecular biology and translational science, 117, 2013, p579-614 , Journal Article, PUBLISHED  DOI
Khan, A.R., Ménétrey, J., Structural biology of arf and rab GTPases' effector recruitment and specificity, Structure , 21, (8), 2013, p1284-1297 , Journal Article, PUBLISHED  TARA - Full Text  DOI
Stack, J., Hurst, T.P., Flannery, S.M., (...), Khan, A.R., Bowie, A.G. , Poxviral protein A52 stimulates p38 mitogen-activated protein kinase (MAPK) activation by causing tumor necrosis factor receptor-associated factor 6 (TRAF6) self-association leading to transforming growth factor β-activated kinase 1 (TAK1) recruitment, Journal of Biological Chemistry, 288, (47), 2013, p33642-33653 , Journal Article, PUBLISHED  DOI

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Award Date
Research Grant - SFI Frontiers Programme 2005
Cyril M. Kay Book Prize in Biochemistry University of Alberta 1995
Studentship, Medical Research Council of Canada 1996
Student Travel Award, American Crystallographic Association St. Louis, MI 1997
Finn Wold Travel Award, Eleventh Symposium of the Protein Society, Boston, MA 1997
Dissertation Fellowship, University of Alberta 1998
Graduate Student Poster Prize, CFBS Annual Meeting Edmonton, Alberta 1998
Fellowship, Human Frontiers Science Program 1999
Fellowship, Centre National de la Recherche Scientifique (CNRS), France 2001
Fellowship, Canadian Institutes of Health Research (CIHR) 2002
Research Grant, Scientific Investigator Programme, Science Foundation Ireland 2004
The experimental goal is determination of structures of Rabs with their effector proteins by X-ray crystallography. The first project will involve Rab6, which regulates the forward and retrograde transport pathways at the level of Golgi membranes. The downstream effects of Rab6 are mediated by Rab6IP1, a 1263-residue Rab6IP1 that contains several novel domains for which there is no structural information in the Protein Data Bank. The second project involves Rab11, which is involved in endocytic recycling processes, as well as endosome-to-Golgi trafficking. One of its effectors is FIP2, which belongs to a family of proteins that contain a conserved C-terminal Rab-binding domain. The structures of these effectors may have novel folds, and the complexes with their respective Rabs are likely to demonstrate novel modes of interaction. In addition, the structure of the complex will enable a generalization of the mechanism of Rab family-mediated signaling, since the domains observed in Rab6IP1 are also found in a variety of other mammalian proteins.