Zobrazeno 1 - 6
of 6
pro vyhledávání: '"P S, Brzovic"'
Autor:
Kedar Puvar, Shalini Iyer, Jiaqi Fu, Sebastian Kenny, Kristos I. Negrón Terón, Zhao-Qing Luo, Peter S. Brzovic, Rachel E. Klevit, Chittaranjan Das
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
The Legionella pneumophila effector MavC inhibits the human ubiquitin-conjugating enzyme Ube2N. Here, the authors combine NMR, X-ray crystallography and biochemical assays and show that MavC catalyses the intramolecular transglutaminase reaction betw
Externí odkaz:
https://doaj.org/article/648e9d96e29748c9b52e0dbcb435943c
Autor:
Anna M. Kolodziejek, Melissa A. Altura, Junping Fan, Erik M. Petersen, Matthew Cook, Peter S. Brzovic, Samuel I. Miller
Publikováno v:
Cell Reports, Vol 27, Iss 7, Pp 2147-2156.e5 (2019)
Summary: Intracellular Salmonella use a type III secretion system (TTSS) to translocate effector proteins across the phagosome membrane and thus promote vacuole membrane tubulation, resulting in intracellular survival. This work demonstrates that the
Externí odkaz:
https://doaj.org/article/b601ce380b8f420ea55a922f7f2a0a92
Publikováno v:
Nature structural biology. 8(10)
The RING domain of the breast and ovarian cancer tumor suppressor BRCA1 interacts with multiple cognate proteins, including the RING protein BARD1. Proper function of the BRCA1 RING domain is critical, as evidenced by the many cancer-predisposing mut
Publikováno v:
The Journal of biological chemistry. 276(44)
Cancer-predisposing missense mutations in the RING domain of BRCA1 primarily target Zn(2+)-liganding residues. Here we report on the structural consequences of such mutations introduced into the second Zn(2+) site (Site II) of the BRCA1 RING domain a
Publikováno v:
The Journal of biological chemistry. 274(9)
Breast cancer 1 (BRCA1) and BRCA1-associated RING domain 1 (BARD1) are multidomain proteins that interact in vivo via their N-terminal RING finger motif regions. To characterize functional aspects of the BRCA1/BARD1 interaction, we have defined the s
Publikováno v:
Proteins. 26(4)
The insulin hexamer is an allosteric protein exhibiting both positive and negative cooperative homotropic interactions and positive cooperative heterotropic interactions (C. R. Bloom et al., J. Mol. Biol. 245, 324-330, 1995). In this study, detailed