Receptor/virus complexes

Meyer, B., et. al., Hepatitis B virus X-associate protein 2 is a subunit of the unliganded aryl hydrocarbon receptor core complex and exhibits transcriptional enhancer activity, Mol. Cell. Biol., 18, 978, 1998. 

These studies were important in that they represented the first antibody-virus complexes of an enveloped virus, helped identify the location of the receptor-binding region of this family of viruses, and were another example of using antibodies to elucidate viral topography. 

For each of the selected target proteins, a set of 10 pharmacophore models was generated based on receptor-inhibitor complexes from the PDB. The three allosteric sites of hepatitis C virus (HCV) polymerase were represented by three, five, and two models, respectively. Structure-based pharmacophore model generation was performed with the software LIGANDSCOUT using the default settings and... 

The main variation of EM that has been reported is cryo-electron microscopy (GEM). Of the reports on the use of GEM during this review period the most-studied structure is the ribosome (from various organisms) and its associated machinery. There have also been a number of studies on various viruses. Other studies that have been reported include ribonucleoproteins, the RNA guide surveillance complex from E.coli, a p53 tetramer bound to a DNA-encoding transcription factor response element, human RXR/VDR nuclear receptor in complex with its DR3 target DNA, a complex (UPF-EJG) from eukaryotic nonsense-mediated mRNA decay,and of a DNA origami structure. ... 

Watowich, S.I., et al. Crystal structures of influenza virus haemagglutinin in complex with high affinity receptor analogs. Structure 2 719-731, 1994. 

Varghese IN, Colman PM (1991) Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 A resolution. 1 Mol Biol 221 473 86 Varghese IN, Laver WG, Colman PM (1983) Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303 35 0 Varghese IN, McKimm-Breschkin IL, Caldwell IB, Kortt AA, Colman PM (1992) The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14 327-332... 

Abstract The entry of viruses into target cells involves a complex series of sequential steps, with opportunities for inhibition at every stage. Entry inhibitors exert their biological properties by inhibiting protein-protein interactions either within the viral envelope (Env) glycoproteins or between viral Env and host-cell receptors. The nature of resistance to entry inhibitors also differs from compounds inhibiting enzymatic targets due to their different modes of action and the relative variability in... 

Attachment There is a high specificity in the interaction between virus and host. The most common basis for host specificity involves the attachment process. The virus particle itself has one or more proteins on the outside which interact with specific cell surface components called receptors. The receptors on the cell surface are normal surface components of the host, such as proteins, polysaccharides, or lipoprotein-polysaccharide complexes, to which the virus particle attaches. In the absence of the receptor site, the virus cannot adsorb, and hence cannot infect. If the receptor site is altered, the host may become resistant to virus infection. However, mutants of the virus can also arise which are able to adsorb to resistant hosts. 

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