Výsledky vyhledávání - "Peter J. Domaille"

Structure of the Minimal Interface Between ApoE and LRP

Autor: Elizabeth A. Komives, J. Helena Prieto, Tracy M. Handel, Miklos Guttman, Peter J. Domaille

Publikováno v: Journal of Molecular Biology. 398:306-319

Clusters of complement-type ligand-binding repeats (CRs) in the low-density lipoprotein receptor (LDLR) family are thought to mediate the interactions with their various ligands. Apolipoprotein E (ApoE), a key ligand for cholesterol homeostasis, has

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91ec29d5916e2ae901571af963448e23
https://doi.org/10.1016/j.jmb.2010.03.022

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Hepatitis C Virus NS3 Protease Requires Its NS4A Cofactor Peptide for Optimal Binding of a Boronic Acid Inhibitor as Shown by NMR

Autor: Zhongren J. Wu, Daniel M. Camac, Peter J. Domaille, Zelda R. Wasserman, Sharon J. Archer, Lawrence J. Mersinger, Charles A. Kettner, Christopher J. Rizzo, Marina Bukhtiyarova, Sharada Jagannathan, Neil A. Farrow

Publikováno v: Chemistry & Biology. 9(1):79-92

NMR spectroscopy was used to characterize the hepatitis C virus (HCV) NS3 protease in a complex with the 24 residue peptide cofactor from NS4A and a boronic acid inhibitor, Ac-Asp-Glu-Val-Val-Pro-boroAlg-OH. Secondary-structure information, NOE const

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[Untitled]

Autor: Julie C. Lougheed, Peter J. Domaille, Tracy M. Handel

Publikováno v: Journal of Biomolecular NMR. 22:211-223

Melanoma inhibitory activity (MIA) is a small secreted protein that is implicated in cartilage cell maintenance and melanoma metastasis. It is representative of a recently discovered family of proteins that contain a Src Homologous 3 (SH3) subdomain.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::39f4dc58dc0132c6851f48927411950a
https://doi.org/10.1023/a:1014961408029

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Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy

Autor: Peter J. Domaille, Chong Hwan Chang, Andrew P. Hinck, Linda K. Nicholson, Yun Xing Wang, Joshua D. Kaufman, Toshimasa Yamazaki, Stephen J. Stahl, Paul T. Wingfield, Patrick Y.S. Lam, Dennis A. Torchia

Publikováno v: Protein Science. 5:495-506

The three-dimensional solution structure of the HIV-1 protease homodimer, MW 22.2 kDa, complexed to a potent, cyclic urea-based inhibitor, DMP323, is reported. This is the first solution structure of an HIV protease/inhibitor complex that has been el

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::93ec2eea15484a30ddac64848f3d176e
https://doi.org/10.1002/pro.5560050311

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An Approach to the Structure Determination of Larger Proteins Using Triple Resonance NMR Experiments in Conjunction with Random Fractional Deuteration

Autor: R. William Broadhurst, Mark J. S. Kelly, Yutaka Ito, James Keeler, Daniel Nietlispach, and Peter J. Domaille, Robin T. Clowes, Hartmut Oschkinat, Jennifer Ashurst, Ernest D. Laue

Publikováno v: Journal of the American Chemical Society. 118:407-415

A combination of simulation and experiment is used to demonstrate that the sensitivity of a family of 3D/4D NMR experiments used to assign resonances and to obtain structural restraints in proteins is improved by partial random deuteration; the impro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::006aa79a45a90c1c0cc4ef01b784179e
https://doi.org/10.1021/ja952207b

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Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C,15N) NMR Spectroscopy

Autor: David F. Lowry, James E. Krywko, Frederick W. Dahlquist, Peter J. Domaille, Philip Matsumura, Franklin J. Moy

Publikováno v: Biochemistry. 33:10731-10742

NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue protein involved in regulating bacterial chemotaxis. Heteronuclear three- and four-dimensional (3D and 4D) experiments have provided sequence-specific resonance

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d95db91fd81ba0a34322a6f0af39ccc0
https://doi.org/10.1021/bi00201a022

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Solution Structure and Dynamics of Ras p21.cntdot.GDP Determined by Heteronuclear Three- and Four-Dimensional NMR Spectroscopy

Autor: S. L. Campbell-Burk, Ernest D. Laue, Peter J. Domaille, T Van Aken, P. J. Kraulis

Publikováno v: Biochemistry. 33:3515-3531

A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the product of the human ras protooncogene and a member of a ubiquitous eukaryo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e80dad7aa340a3463cd930ffa4f62435
https://doi.org/10.1021/bi00178a008

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Secondary structure and signal assignments of human-immunodeficiency-virus-1 protease complexed to a novel, structure-based inhibitor

Autor: Peter J. Domaille, Toshimasa Yamazaki, Dennis A. Torchia, Paul T. Wingfield, Sharon Campbell-Burk, Linda K. Nicholson, Joshua D. Kaufman, Stephan J. Stahl

Publikováno v: European Journal of Biochemistry. 219:707-712

We report comprehensive NMR studies in solution of the human-immunodeficiency-virus (HIV)-1 protease. Stable solutions of the protease were obtained by complexing the protein to a designed cyclic urea inhibitor DMP 323. A variety of triple-resonance

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b16b8240d499d9484f7bc524b4139f4
https://doi.org/10.1111/j.1432-1033.1994.tb19987.x

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A 4D HCC(CO)NNH experiment for the correlation of aliphatic side-chain and backbone resonances in 13C/15N-labelled proteins

Autor: Peter J. Domaille, C. H. Hardman, Ernest D. Laue, Wayne Boucher, Robin T. Clowes

Publikováno v: Journal of Biomolecular NMR. 3:349-354

We recently proposed a novel four-dimensional (4D) NMR strategy for the assignment of backbone nuclei in spectra of 13C/15N-labelled proteins (Boucher et al. (1992) J. Am. Chem. Soc., 114, 2262–2264 and J. Biomol. NMR, 2, 631–637). In this paper

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::04fdcf37f87b5cbee556bcaaa2bd716d
https://doi.org/10.1007/bf00212520

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