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PDB-101: Molecule of the Month: SARS-CoV-2 Spike Spike protein from SARS-CoV, with one receptor binding domain (RBD) in the up position, and a closed conformation of the SARS-CoV-2 spike The S1 fragment is shown in magenta and the S2 fragment in red, with glycosylation in lighter shades
RCSB PDB - 8ZER: Crystal structure of the complex of Wuhan SARS-CoV-2 . . . Here we report on the successful crystal structure determination of the RBD:P2C5 complex at 3 1 Å, which revealed the intricate protein-protein interface, sterically occluding full ACE2 receptor binding by the P2C5-neutralized RBD
RCSB PDB - 7UZC: Structure of the SARS-CoV-2 RBD in complex with the . . . Immunization with nanoparticles co-displaying spike receptor-binding domains (RBDs) from eight sarbecoviruses (mosaic-8 RBD-nanoparticles) efficiently elicits cross-reactive polyclonal antibodies against conserved sarbecovirus RBD epitopes
5DO2: Complex structure of MERS-RBD bound with 4C2 antibody - RCSB PDB Both mAbs potently bind to MERS-RBD and block virus entry in vitro with high efficacy We further investigated their mechanisms of neutralization by crystallizing the complex between the Fab fragments and the RBD, and solved the structure of the 4C2 Fab MERS-RBD complex
RCSB PDB - 7UB0: SARS-CoV-2 Omicron-BA. 2 3-RBD down Spike Protein . . . BA 2 receptor-binding domain (RBD) mutations induce remodeling of the RBD structure, resulting in tighter packing and improved thermostability Interprotomer RBD interactions are enhanced in the closed (or 3-RBD-down) BA 2 S, while the fusion peptide is less accessible to antibodies than in BA 1
RCSB PDB - 8IDN: Cryo-EM structure of RBD E77-Fab complex Antibodies that target the receptor-binding domain (RBD) of S have high potency in preventing viral infection The ongoing evolution of SARS-CoV-2, especially mutations occurring in the RBD of new variants, has severely challenged the development of neutralizing antibodies and vaccines