Zbyszek Otwinowski
University of Texas Southwestern Medical Center
127 Papers
575 Citations
Zbyszek Otwinowski is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Biology & Protein structure. The author has an hindex of 43, co-authored 115 publications. Previous affiliations of Zbyszek Otwinowski include University of Illinois at Chicago & University of Texas at Dallas.
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Papers
Secondary Structure of Huntingtin Amino-Terminal Region
TL;DR: It is proposed that the pathogenic polyQ expansion in the Htt protein increases the length of the random coil, which promotes aggregation and facilitates abnormal interactions with other proteins in cells.
277
Crystal structure of the human sterol transporter ABCG5/ABCG8
Jyh-Yeuan Lee,Lisa N. Kinch,Lisa N. Kinch,Dominika Borek,Jin Wang,Junmei Wang,Ina L. Urbatsch,Xiao Song Xie,Nikolai V. Grishin,Jonathan C. Cohen,Zbyszek Otwinowski,Helen H. Hobbs,Daniel M. Rosenbaum +12 more
TL;DR: The G5G8 structure provides a mechanistic framework for understanding sterol transport and the disruptive effects of mutations causing sitosterolaemia, and reveals a new transmembrane fold that is present in a large and functionally diverse superfamily of ABC transporters.
259
The 2.4 A crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S.
TL;DR: The crystal structure of GroEL with ATPγS bound to each subunit shows that ATP binds to a novel pocket, whose primary sequence is highly conserved among chaperonins.
242
The crystal structure of trp aporepressor at 1.8 Å shows how binding tryptophan enhances DNA affinity
Rongguang Zhang,Rongguang Zhang,Andrzej Joachimiak,Andrzej Joachimiak,Catherine L. Lawson,Richard W. Schevitz,Zbyszek Otwinowski,Paul B. Sigler +7 more
TL;DR: Comparison of the crystal structure of inactive unliganded trp aporepressor with that of trp repressor shows that binding tryptophan activates the dimer a thousandfold by moving two symmetrically-disposed flexible bihelical motifs.
238
An intrinsically disordered peptide from ebola virus VP35 controls viral RNA synthesis by modulating nucleoprotein-RNA interactions
Daisy W. Leung,Dominika Borek,Priya Luthra,Jennifer M. Binning,Manu Anantpadma,Gai Liu,Ian B. Harvey,Zhaoming Su,Ariel C. Endlich-Frazier,Juanli Pan,Reed S. Shabman,Wah Chiu,Robert A. Davey,Zbyszek Otwinowski,Christopher F. Basler,Gaya K. Amarasinghe +15 more
TL;DR: The structure of the NPBP/ΔNPNTD complex, solved to 3.7 Å resolution, reveals how NPBP peptide occludes a large surface area that is important for NP-NP and NP-RNA interactions and for viral RNA synthesis.
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