Unliganded HIV-1 gp120 core structures assume the CD4-bound conformation with regulation by quaternary interactions and variable loops

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 109; no. 15; pp. 5663 - 5668
• Main Authors: 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, Debnath, Asim K, Shapiro, Lawrence, Bewley, Carole A, Mascola, John R, Sodroski, Joseph G, Kwong, Peter D
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 10.04.2012; National Acad Sciences
• Subjects: 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

The HIV-1 envelope (Env) spike (gp1203/gp413) undergoes considerable structural rearrangements to mediate virus entry into cells and to evade the host immune response. Engagement of CD4, the primary human receptor, fixes a particular conformation and primes Env for entry. The CD4-bound state, howeve...