Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops - Kwon, Young Do; Finzi, Andrés; Wu, Xueling; Dogo-Isonagie, Cajetan; Lee, Lawrence K; Moore, Lucas R; Schmidt, Stephen D; Stuckey, Jonathan; Yang, Yongping; Zhou, Tongqing; Zhu, Jiang; Vicic, David A; et al. (Proceedings of the National Academy of Sciences - PNAS, 2012)
Keywords: 60 APPLIED LIFE SCIENCES; ANTIBODIES; Biochemistry; Biological Sciences; CAPACITY; CD4 antigen; CD4 Antigens; CD4 Antigens - metabolism; Cells; chemistry; Conformation; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; Deformation; Envelopes; Glycoprotein gp120; Glycoproteins; HEK293 Cells; HIV; HIV 1; HIV Envelope Protein gp120; HIV Envelope Protein gp120 - chemistry; HIV Envelope Protein gp120 - metabolism; Human immunodeficiency virus; Human immunodeficiency virus 1; Humans; Immune response; INACTIVATION; Ligands; metabolism; Models, Molecular; Molecular structure; Neutralization; Protein Binding; Protein Structure, Quaternary; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors; REGULATIONS; RESTRAINTS; Solutions; Structure-Activity Relationship; THERMODYNAMICS; Viral morphology; Viruses