18 research outputs found
Synthesis and crystal structures of two new (Te, N,) type hybrid organotellurium ligands
No full textNeutralizing antibody to human rhinovirus 14 penetrates the receptor-binding canyon
No full textThe three-dimensional structure of intact human rhinovirus 14 (HRV-14) complexed with Fab fragments (Fab17-IA) from a strongly neutralizing antibody that binds bivalently to the virion(1,2) has been determined to 4.0 Å resolution by a combination of X-ray crystallography and cryo-electron microscopy. In contradiction to the most commonly held model of antibody-mediated neutralization, Fab17-IA does not induce a conformational change in the HRV-14 capsid. Instead, the paratope of the antibody undergoes a large conformational change to accommodate the epitope. Unlike any previously described antibody–antigen structure, the conserved framework region of the antibody makes extensive contact with the viral surface. Fab17-IA penetrates deep within the canyon in which the cellular receptor for HRV-14 binds(3,4). Hence, it is unlikely that viral quaternary structure evolves merely to evade immune recognition. Instead, the shape and position of the receptor-binding region on a virus probably dictates receptor binding and subsequent uncoating events and has little or no influence on concealing the virus from the immune system
Structural Basis of the Unusual Stability and Substrate Specificity of Ervatamin C, a Plant Cysteine Protease from Ervatamia coronaria
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Structure-Based Design of a Parallel Synthetic Array Directed Toward the Discovery of Irreversible Inhibitors of Human Rhinovirus 3C Protease
No full textCrystal structure of TRAF1 TRAF domain and its implications in the TRAF1-mediated intracellular signaling pathway
No full textNaked d-orbital in a centrochiral Ni(II) complex as a catalyst for asymmetric [3+2] cycloaddition
No full textFirst Brønsted Acid-Induced Ring Expansion of an Oxaphosphirane Complex: A Combined Experimental and DFT Study
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