Istvan Botos, Ph.D.

Photo of Istvan Botos
Scientific Focus Areas: Structural Biology

Publications

A selection of recent and significant publications can be viewed below.

Insertion of proteins and lipopolysaccharide into the bacterial outer membrane.
Botos I, Noinaj N, Buchanan SK.
Philos Trans R Soc Lond B Biol Sci (2017 Aug 5) 372. Abstract/Full Text
Structure and dynamics of a constitutively active neurotensin receptor.
Krumm BE, Lee S, Bhattacharya S, Botos I, White CF, Du H, Vaidehi N, Grisshammer R.
Sci Rep (2016 Dec 7) 6:38564. Abstract/Full Text
Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.
Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N.
Structure (2016 Dec 6) 24:2127-2137. Abstract/Full Text
Structural insight into the role of the Ton complex in energy transduction.
Celia H, Noinaj N, Zakharov SD, Bordignon E, Botos I, Santamaria M, Barnard TJ, Cramer WA, Lloubes R, Buchanan SK.
Nature (2016 Oct 6) 538:60-65. Abstract/Full Text
Structural and Functional Characterization of the LPS Transporter LptDE from Gram-Negative Pathogens.
Botos I, Majdalani N, Mayclin SJ, McCarthy JG, Lundquist K, Wojtowicz D, Barnard TJ, Gumbart JC, Buchanan SK.
Structure (2016 Jun 7) 24:965-976. Abstract/Full Text
The structural biology of Toll-like receptors.
Botos I, Segal DM, Davies DR.
Structure (2011 Apr 13) 19:447-59. Abstract/Full Text
The toll-like receptor 3:dsRNA signaling complex.
Botos I, Liu L, Wang Y, Segal DM, Davies DR.
Biochim Biophys Acta (2009 Sep-Oct) 1789:667-74. Abstract/Full Text
Structural basis of toll-like receptor 3 signaling with double-stranded RNA.
Liu L, Botos I, Wang Y, Leonard JN, Shiloach J, Segal DM, Davies DR.
Science (2008 Apr 18) 320:379-81. Abstract/Full Text
Limited proteolysis of E. coli ATP-dependent protease Lon - a unified view of the subunit architecture and characterization of isolated enzyme fragments.
Melnikov EE, Andrianova AG, Morozkin AD, Stepnov AA, Makhovskaya OV, Botos I, Gustchina A, Wlodawer A, Rotanova TV.
Acta Biochim Pol (2008) 55:281-96. Abstract/Full Text
The expanding diversity of serine hydrolases.
Botos I, Wlodawer A.
Curr Opin Struct Biol (2007 Dec) 17:683-90. Abstract/Full Text
Atomic-resolution crystal structure of the antiviral lectin scytovirin.
Moulaei T, Botos I, Ziółkowska NE, Bokesch HR, Krumpe LR, McKee TC, O'Keefe BR, Dauter Z, Wlodawer A.
Protein Sci (2007 Dec) 16:2756-60. Abstract/Full Text
[Forms of LonB protease from Archaeoglobus fulgidus devoid of the transmembrane domain: the contribution of the quaternary structure to the regulation of enzyme proteolytic activity].
Makhovskaia OV, Kozlov S, Botos I, Stepnov AA, Andrianova AG, Gushchina AE, Vlodaver A, Mel'nikov EE, Rotanova TV.
Bioorg Khim (2007 Nov-Dec) 33:657-60. Abstract/Full Text
Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
Rotanova TV, Botos I, Melnikov EE, Rasulova F, Gustchina A, Maurizi MR, Wlodawer A.
Protein Sci (2006 Aug) 15:1815-28. Abstract/Full Text
Overexpression and purification of scytovirin, a potent, novel anti-HIV protein from the cultured cyanobacterium Scytonema varium.
Xiong C, O'Keefe BR, Botos I, Wlodawer A, McMahon JB.
Protein Expr Purif (2006 Apr) 46:233-9. Abstract/Full Text
The molecular structure of the TLR3 extracellular domain.
Bell JK, Botos I, Hall PR, Askins J, Shiloach J, Davies DR, Segal DM.
J Endotoxin Res (2006) 12:375-8. Abstract/Full Text
Atomic-resolution crystal structure of the proteolytic domain of Archaeoglobus fulgidus lon reveals the conformational variability in the active sites of lon proteases.
Botos I, Melnikov EE, Cherry S, Kozlov S, Makhovskaya OV, Tropea JE, Gustchina A, Rotanova TV, Wlodawer A.
J Mol Biol (2005 Aug 5) 351:144-57. Abstract/Full Text
The molecular structure of the Toll-like receptor 3 ligand-binding domain.
Bell JK, Botos I, Hall PR, Askins J, Shiloach J, Segal DM, Davies DR.
Proc Natl Acad Sci U S A (2005 Aug 2) 102:10976-80. Abstract/Full Text
Pathological crystallography: case studies of several unusual macromolecular crystals.
Dauter Z, Botos I, LaRonde-LeBlanc N, Wlodawer A.
Acta Crystallogr D Biol Crystallogr (2005 Jul) 61:967-75. Abstract/Full Text
Proteins that bind high-mannose sugars of the HIV envelope.
Botos I, Wlodawer A.
Prog Biophys Mol Biol (2005 Jun) 88:233-82. Abstract/Full Text
Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains.
Rotanova TV, Melnikov EE, Khalatova AG, Makhovskaya OV, Botos I, Wlodawer A, Gustchina A.
Eur J Biochem (2004 Dec) 271:4865-71. Abstract/Full Text
Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.
Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A.
J Struct Biol (2004 Apr-May) 146:113-22. Abstract/Full Text
The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.
Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A.
J Biol Chem (2004 Feb 27) 279:8140-8. Abstract/Full Text
Cyanovirin-N: a sugar-binding antiviral protein with a new twist.
Botos I, Wlodawer A.
Cell Mol Life Sci (2003 Feb) 60:277-87. Abstract/Full Text
Structures of the complexes of a potent anti-HIV protein cyanovirin-N and high mannose oligosaccharides.
Botos I, O'Keefe BR, Shenoy SR, Cartner LK, Ratner DM, Seeberger PH, Boyd MR, Wlodawer A.
J Biol Chem (2002 Sep 13) 277:34336-42. Abstract/Full Text
Domain-swapped structure of a mutant of cyanovirin-N.
Botos I, Mori T, Cartner LK, Boyd MR, Wlodawer A.
Biochem Biophys Res Commun (2002 May 31) 294:184-90. Abstract/Full Text
The domain-swapped dimer of cyanovirin-N is in a metastable folded state: reconciliation of X-ray and NMR structures.
Barrientos LG, Louis JM, Botos I, Mori T, Han Z, O'Keefe BR, Boyd MR, Wlodawer A, Gronenborn AM.
Structure (2002 May) 10:673-86. Abstract/Full Text
Crystal structures of the semireduced and inhibitor-bound forms of cyclic nucleotide phosphodiesterase from Arabidopsis thaliana.
Hofmann A, Grella M, Botos I, Filipowicz W, Wlodawer A.
J Biol Chem (2002 Jan 11) 277:1419-25. Abstract/Full Text
Crystal structure of a cyclic form of bovine pancreatic trypsin inhibitor.
Botos I, Wu Z, Lu W, Wlodawer A.
FEBS Lett (2001 Nov 30) 509:90-4. Abstract/Full Text
The structure of an insect chymotrypsin.
Botos I, Meyer E, Nguyen M, Swanson SM, Koomen JM, Russell DH, Meyer EF.
J Mol Biol (2000 May 19) 298:895-901. Abstract/Full Text
Structure of recombinant mouse collagenase-3 (MMP-13).
Botos I, Meyer E, Swanson SM, Lemaître V, Eeckhout Y, Meyer EF.
J Mol Biol (1999 Oct 1) 292:837-44. Abstract/Full Text
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Botos I, Scapozza L, Zhang D, Liotta LA, Meyer EF.
Proc Natl Acad Sci U S A (1996 Apr 2) 93:2749-54. Abstract/Full Text
Structure-based analysis of inhibitor binding to Ht-d.
Botos I, Scapozza L, Shannon JD, Fox JW, Meyer EF.
Acta Crystallogr D Biol Crystallogr (1995 Jul 1) 51:597-604. Abstract/Full Text
Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d).
Zhang D, Botos I, Gomis-Rüth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF.
Proc Natl Acad Sci U S A (1994 Aug 30) 91:8447-51. Abstract/Full Text

Books and Book Chapters

"Toll-like receptors – Structure and signaling."
Botos I, Davies DR.
Handbook of Cell Signaling. Bradshaw, ed.
Academic Press. (2009) 139-143.
"Snake venom metalloproteinases (SVMPs): Functional modulation of activity by non-proteinase domains and the structural relationship of these proteins to mammalian homologs."
Bjarnason JB, Botos I, Fox JW, Jia LG, Meyer EF
The astacins. Zwilling R, Stocker W, eds.
(1995) 349-361, Dr. Kovac, Hamburg.
Backwards binding and other structural surprizes.
Botos I, Meyer EF, Scapozza L, Zhang D.
Perspect. Drug Discovery Des. 3, (1995) 168-195.