有哪些信誉好的足球投注网站crystal structure of the neutralizing llama vhh d7 and its mode of hiv-1 gp120 interaction晶体结构的中和骆驼vhh d7及其hiv - 1抗体来源于交互模式.pdfVIP
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crystal structure of the neutralizing llama vhh d7 and its mode of hiv-1 gp120 interaction晶体结构的中和骆驼vhh d7及其hiv - 1抗体来源于交互模式
Crystal Structure of the Neutralizing Llama VHH D7 and Its Mode of HIV-1 gp120 Interaction 1 1,2 3 3 1,4 Andreas Hinz , David Lutje Hulsik , Anna Forsman , Willie Wee-Lee Koh , Hassan Belrhali , Andrea 2 2 3 2 1 Gorlani , Hans de Haard , Robin A. Weiss , Theo Verrips , Winfried Weissenhorn * ´ 1 Unit of Virus Host Cell Interactions (UVHCI), UMI 3265, Universite Joseph Fourier-EMBL-CNRS, Grenoble, France, 2 Department of Cellular Architecture and Dynamics, University of Utrecht, Utrecht, The Netherlands, 3 Division of Infection and Immunity, MRC/UCL Centre for Medical Molecular Virology, University College London, London, United Kingdom, 4 European Molecular Biology Laboratory, Grenoble, France Abstract HIV-1 entry into host cells is mediated by the sequential binding of the envelope glycoprotein gp120 to CD4 and a chemokine receptor. Antibodies binding to epitopes overlapping the CD4-binding site on gp120 are potent inhibitors of HIV entry, such as the llama heavy chain antibody fragment VHH D7, which has cross-clade neutralizing properties and ˚ competes with CD4 and mAb b12 for high affinity binding to gp120. We report the crystal structure of the D7 VHH at 1.5 A resolution, which reveals the molecular details of the complementarity determining regions (C
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