About: [Image: see text] Four of five different monoclonal antibodies (mAbs) that have been crystallized in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein (S) have remarkably similar primary and secondary loop structures at the heavy chain complementarity-determining regions (HCDR) 1 and 2. All these reports give a structural basis for the deceptively difficult problem of accurate peptidomimetic loop mimic design.   Goto Sponge  NotDistinct  Permalink

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  • [Image: see text] Four of five different monoclonal antibodies (mAbs) that have been crystallized in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike protein (S) have remarkably similar primary and secondary loop structures at the heavy chain complementarity-determining regions (HCDR) 1 and 2. All these reports give a structural basis for the deceptively difficult problem of accurate peptidomimetic loop mimic design.
Subject
  • Virology
  • Immunology
  • Biotechnology
  • Proteins
  • Immune system
  • Biomolecules
  • Monoclonal antibodies
  • Therapeutic antibodies
  • Cell signaling
  • Cancer treatments
  • Chemical bonding
  • Ligands (biochemistry)
  • Molecular biology
  • Reagents for biochemistry
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