Faculty

Jinwoo Ahn
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Phone (412) 383-6933
Fax (412) 648-9008

University of Pittsburgh
1055 Biomedical Science Tower 3

JInwoo Ahn

Associate Professor

Protein-protein and protein-ligand interactions are major events in many critical biological pathways. My research focuses on investigating the molecular and structural basis of these interactions. To that end, I utilize molecular biology and protein biochemistry approaches to obtain functionally active recombinant proteins. With those, we reconstitute and monitor biological events in vitro to directly correlate protein structure-function with biological outcome. We utilize various bioanalytical and biophysical methodology including, but not limited to, CD, fluorescence, SEC-MALS, ITC, SPR, SWAX and HPLC as well as conventional biochemistry. We are currently studying HIV virulence factor-host protein interactions, Cullin-based E3 ubiquitin ligase assembly, regulation of tumor suppressor p53 and its homologs functions by repressors and activators.

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Education & Training

Undergraduate
Yonsei University, Seoul, Korea
B.S. 1991 in Chemistry

Graduate
The Ohio State University
Ph.D., 1997 in Chemistry

Postgraduate
Columbia University, New York
Postdoctoral Associate 1997 – 2003

Representative Publications

Zhou, X., Delucia, M., Hao, C., Hrecka, K., Monnie, C., Skowronski, J., Ahn, J. HIV-1 Vpr protein directly loads Helicase-like transcription factor (HLTF) onto the CRL4-DCAF1 E3 ubiquitin ligase. J. Biol. Chem. 292, 21117-21127 (2017)

Jang, S., Zhou, X., Ahn, J. Substrate specificity of SAMHD1 triphosphohydrolase activity is controlled by deoxyribonucleoside triphosphates and phosphorylation at Thr592. Biochemistry 55, 5635-5646 (2016)

Zhou, X., DeLucia, M., Ahn, J. SLX4/SLX1 independent downregulation of MUS81/EME1 by HIV-1 Vpr. J. Biol. Chem. 291, 16936-16947 (2016)

Wu, Y, Koharudin, L., Mehrens, J., DeLucia, M., Byeon, C.-H., Byeon, I.J., Calero, G., Ahn, J., and Gronenborn, A. M., Structural basis of clade-specific engagement of SAMHD1 restriction factors by lentiviral Vpx virulence factors.. J. Biol. Chem. 290, 17935-45 (2105)

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Active Grants

University of Pittsburgh Center for HIV Protein Interactions (PCHPI), Core director and Project Leader
8/1/17 – 7/31/22
NIH P50GM082251

Structure and function relationships regulating SAMHD1’s dual enzymatic activities, Principal Investigator
7/1/15 – 6/30/20
NIH R01GM116642

The molecular basis of cardiolipin-protein interactions implicated in intrinsic apoptosis, Co-Investigator
9/1/16 – 8/31/20
NIH R01GM113908

Imaging of single HIV-1 uncoating and transport to the nucleus, Co-Investigator
3/24/17 – 2/28/22
NIH R01AI129862

James Conway
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Phone (412) 383-9847
Fax (412) 648-8998

University of Pittsburgh
2047 Biomedical Science Tower 3

James Conway

Associate Professor
Department of Structural Biology

Study the structure and function of macromolecular complexes, such as virus capsids, using cryo-electron microscopy and combining this with subunit atomic models to extend interpretation into details of the protein folds and interfaces. Particular systems being studied include herpesviruses and dsDNA bacteriophages such as HK97, SPO1, T5 and others, These tailed phages have important structural similarities with each other and also with animal viruses such as herpesvirus, suggesting that there may be a long evolutionary connection between them. The dynamic aspects of the virus lifecycle – assembly, DNA packaging, infection and DNA delivery – are often better suited to cryoEM study than crystallography. Although current resolutions achieved for icosahedral capsids are between 10-20Å, this is steadily improving as new procedures are developed, such as automated data collection and high-speed data analysis. Lower symmetry structures, such as entire virus or phage particles, requires more data and achieve lower resolution but also benefit from these advances. Ultimately, we aim to characterize the structural and functional repertoire of a virus throughout its lifecycle, which will have benefits in understanding protein-protein and protein-DNA interactions as well as the evolution of protein structure, and in developing new targets for interfering with viral infection and replication, and technological application of the knowledge.

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Education & Training

Undergraduate
Massey University, Palmerstrom, North New Zealand
B.S. 1985 in Physics

Graduate
Massey University, Palmerston North New Zealand
Ph.D. 1989 in Biophysics

Postgraduate
National Institues of Health
Bethesda, MD 1990 - 1996

Awards & Honors

1986 Fibrous Proteins Merit Award, Massey University
1997 Special Achievement Award, NIAMS/NIH, In recognition and appreciation of special achievement
1998 Group Merit Award, NIAMS/NIH, In recognition of pioneering contributions to image processing, advancing the resolution attainable in biological electron microscopy

Representative Publications

Lee H, Brendle SA, Bywaters SM, Guan J, Ashley RE, Yoder JD, Makhov AM, Conway JF, Christensen ND & Hafenstein S. A CryoEM study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment. J Virol 89, 1428-1438, 2015

Shingler KL, Cifuente JO, Ashley RE, Makhov AM, Conway JF & Hafenstein S. The enterovirus 71 procapsid binds neutralizing antibodies and rescues virus infection in vitro. J Virol 89, 1900-1908, 2015.

Sattar S, Bennett NJ, Wen WX, Guthrie JM, Blackwell LF, Conway JF & Rakonjac J. Ff-nano, short functionalized nanorods derived from Ff (f1, fd or M13) filamentous bacteriophage. Frontiers in Microbiology (Virology) 6, 316, 2015.

Guan J, Bywaters SM, Brendle SA, Lee H, Ashley RE, Makhov AM, Conway JF, Christensen ND & Hafenstein S. Structural comparison of four different antibodies interacting with human papillomavirus 16 and mechanisms of neutralization. Virology 483, 253-263, 2015.

Tandon R, Mocarski ES and Conway JF. The A, B, Cs of herpesvirus capsids. Viruses 7, 899-914. 2015.

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Active Grants

Direct Electron Detecting (DED) Camer
04/01/15 – 03/31/16
National Institutes of Health
S10

Structure and Function of the Herpesvirus Capsid
08/15/11 – 07/31/20
National Institutes of Health
R01

Structural Determinants of Amelogenin Function in Regulating Enamel Formation
09/01/12 – 08/31/17
National Institutes of Health
R01

Inborn Errors of Long Chain Fat Metabolism
07/01/07 – 03/31/16
National Institutes of Health
R01

Roles of Cytomegalovirus Proteins pp150 and pUL96 in Virus Maturation
11/01/14 – 10/31/19
National Institutes of Health
R01

Guillermo Calero
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Phone (412) 383-5319
Fax (412) 648-9008

University of Pittsburgh
1040 Biomedical Science Tower 3

Guillermo Calero

Associate Professor
Department of Structural Biology

My laboratory at the University of Pittsburgh, works on reconstitution of multi-protein complexes (MPCs) for biochemical and X-ray crystallographic studies. In particular we are interested in MPCs involved in: 1) nuclear events such as transcription initiation and DNA repair, and 2) Interactions of membrane receptors with their cytoplasmic partners. Since MPCs cannot be isolated as a whole from cells, we have developed biochemical tools that have allowed us to express and purify individual components (monomeric or multimeric) to reconstitute such MPCs. Our ultimate goals is to crystallize and perform structural studies using X-ray crystallography of these samples which posses great biological interest. We are also participating in development of methods using EM to identify best diffracting nano-crystals for femtosecond diffraction experiments.

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Education & Training

Graduate
Baylor College of Medicine
Facultad de Medicina, UNAM
M.D. 1991

Cornell University
Ph.D. 2003 in Chemistry and Chemical Biology

Postgraduate
Stanford University
Postdoctoral Scholar 2003-2008

Representative Publications

Murakami K, Calero G, Brown CR, Liu X, Davis RE, Boeger H and Kornberg RD (2013). Formation and fate of a complete, 31-Protein, RNA polymerase II transcription initiaition complex. Journal of Biological Chemistry.

Wehbi VL, Stevenson HP, Feinstein TN, Calero G, Romero, G and Vilardaga JP (2013). Non-canonical GPCR signaling arising from a PTH-arrestin-GS complex. Proc Natl Acad Sci U S A. 110(4):1530-5.

Stevenson HP, Mahkov AM, Calero M, Mathews I, Lin G, Santamaria H, Ross TM, Soltis M, Koshla S, Conway J, Cohen A and Calero G (2014). Electron Microscopy Screening of Protein Nano crystals for Serial Femtosecond Crystallography. Proc Natl Acad Sci U S A. 111(23):8470-5.

Stevenson H.P., DePonte D.P., Makhov A.M., Zeldin O.B., Calero G*, and Cohen A.E* (2014). Transmission electron microscopy as a tool for nano-crystal characterization pre- and post-injector. Philosophical Transations B. Philosophical Transactions B. 17;369:1647 * Corresponding author

Calero G, Cohen A.E, Luft J.R and Snell E (2014). Identifying, studying and making good use of macromolecular crystals. Acta Crystallographica F. 70:993-1008

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Active Grants

Structural Studies of RNA Polymerase II Transcription Initiation and Elongation
01/15/15 – 12/31/19
National Institutes of Health
R01

Structural and Functional Mechanisms of PTH-Receptor Signaling
07/01/14 – 05/31/18
National Institutes of Health
R01