Abstract

. In this application three-part approach will be implemented that involves (i) 2 D NMR and structural studies of several of the smaller proteins (including pl, p2, p6 and p7; (ii) NMR and structural studies of p7 oligonucleotide complexes, and (iii) studies of larger proteins (including p17 and p24) using three-dimensional homo- and heteronuclear correlated spectroscopic methods. For 3D NMR studies, isotope-enriched protein samples will be obtained from virus particles grown using 13C- and 15N-enriched media. The investigator believes that understanding the 3D structural details of the HIV-1 proteins is essential for understanding their function, and should facilitate the development of vaccines and new chemotherapeutic approaches for the control of AIDS.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
1R01AI030917-01A1
Application #
3145919
Study Section
AIDS and Related Research Study Section 4 (ARRD)
Project Start
1991-03-01
Project End
1994-02-28
Budget Start
1991-03-01
Budget End
1992-02-29
Support Year
1
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
University of Maryland Balt CO Campus
Department
Type
Schools of Arts and Sciences
DUNS #
City
Baltimore
State
MD
Country
United States
Zip Code
21250

  Publications

Mercredi, Peter Y; Bucca, Nadine; Loeliger, Burk et al. (2016) Structural and Molecular Determinants of Membrane Binding by the HIV-1 Matrix Protein. J Mol Biol 428:1637-55
Tedbury, Philip R; Mercredi, Peter Y; Gaines, Christy R et al. (2015) Elucidating the mechanism by which compensatory mutations rescue an HIV-1 matrix mutant defective for gag membrane targeting and envelope glycoprotein incorporation. J Mol Biol 427:1413-1427
Zhang, Hongtao; Curreli, Francesca; Waheed, Abdul A et al. (2013) Dual-acting stapled peptides target both HIV-1 entry and assembly. Retrovirology 10:136
Checkley, Mary Ann; Luttge, Benjamin G; Mercredi, Peter Y et al. (2013) Reevaluation of the requirement for TIP47 in human immunodeficiency virus type 1 envelope glycoprotein incorporation. J Virol 87:3561-70
Kyere, Sampson K; Mercredi, Peter Y; Dong, Xinhong et al. (2012) The HIV-1 matrix protein does not interact directly with the protein interactive domain of AP-3?. Virus Res 169:411-4
Lu, Kun; Heng, Xiao; Summers, Michael F (2011) Structural determinants and mechanism of HIV-1 genome packaging. J Mol Biol 410:609-33
Summers, Michael F (2011) Training the next generation of protein scientists. Protein Sci 20:1796-801
Hamard-Peron, E; Juillard, F; Saad, J S et al. (2010) Targeting of murine leukemia virus gag to the plasma membrane is mediated by PI(4,5)P2/PS and a polybasic region in the matrix. J Virol 84:503-15
Valentine, Kathleen G; Peterson, Ronald W; Saad, Jamil S et al. (2010) Reverse micelle encapsulation of membrane-anchored proteins for solution NMR studies. Structure 18:9-16
Kyere, Sampson K; Joseph, Prem Raj B; Summers, Michael F (2008) The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct. PLoS One 3:e1902

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