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Probing Oligomerized Conformations of Defensin in the Membrane.

  1. Author:
    Gan, Wenxun
    Schneidman, Dina
    Zhang, Ning
    Ma, Buyong
    Nussinov, Ruth

  2. Author Address

    Research Center of Basic Medical Sciences, Tianjin Medical University, Tianjin, 300060, China., Cancer Institute and Hospital, Tianjin Medical University, Tianjin, 300060, China., Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, CA, 94158, USA., Basic Science Program, Leidos Biomedical Research, Inc., Frederick, MD, 21702, USA., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, 21702, USA., Basic Science Program, Leidos Biomedical Research, Inc., Frederick, MD, 21702, USA. nussinor@helix.nih.gov., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD, 21702, USA. nussinor@helix.nih.gov., Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Sackler Institute of Molecular Medicine, Tel Aviv University, Tel Aviv, 69978, Israel. nussinor@helix.nih.gov.,
    1. Year: 2017
  2. Journal: Methods in molecular biology (Clifton, N.J.)
    1. 1529
    2. Pages: 353-362
  4. Type of Article: Article
  1. Abstract:

    Computational prediction and design of membrane protein-protein interactions facilitate biomedical engineering and biotechnological applications. Due to their antimicrobial activity, human defensins play an important role in the innate immune system. Human defensins are attractive pharmaceutical targets due to their small size, broad activity spectrum, reduced immunogenicity, and resistance to proteolysis. Protein engineering based modification of defensins can improve their pharmaceutical properties. Here we present an approach to computationally probe defensins 39; oligomerization states in the membrane. First, we develop a novel docking and rescoring algorithm. Then, on the basis of the 3D structure of Sapecin, an insect defensin, and a model of its antimicrobial ion-channel, we optimize the parameters of our empirical scoring function. Finally, we apply our docking program and scoring function to the hBD-2 (human ß-defensin-2) molecule and obtain structures of four possible oligomers. These results can be used in higher level simulations.

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  2. DOI: 10.1007/978-1-4939-6637-0_18
  3. PMID: 27914061

Library Notes

  1. Fiscal Year: FY2016-2017
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