1K5M

Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2

Summary for 1K5M

• Entry DOI: 10.2210/pdb1k5m/pdb
• Related: 4rhv
• Descriptor: COAT PROTEIN VP1 (P1D), CHIMERA OF HRV14 COAT PROTEIN VP2 (P1B) AND the V3 loop of HIV-1 gp120, COAT PROTEIN VP3 (P1C), ... (6 entities in total)
• Functional Keywords: engineered rhinovirus, hiv-1 v3 loop, beta turns, icosahedral virus, virus
• Biological source: Human rhinovirus 14; More
• Cellular location: Capsid protein VP0: Virion . Capsid protein VP4: Virion . Capsid protein VP2: Virion . Capsid protein VP3: Virion . Capsid protein VP1: Virion . Protein 2B: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 2C: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3A: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Protein 3AB: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . Viral protein genome-linked: Virion . Protease 3C: Host cytoplasm . Protein 3CD: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side . RNA-directed RNA polymerase: Host cytoplasmic vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side : P03303 P03303 P03303 P03303
• Total number of polymer chains: 4
• Total formula weight: 96377.77

Authors

Ding, J.,Smith, A.D.,Geisler, S.C.,Ma, X.,Arnold, G.F.,Arnold, E. (deposition date: 2001-10-11, release date: 2002-07-17, Last modification date: 2023-08-16)

Primary citation

Ding, J.,Smith, A.D.,Geisler, S.C.,Ma, X.,Arnold, G.F.,Arnold, E.
Crystal Structure of a Human Rhinovirus that Displays Part of the HIV-1 V3 Loop and Induces Neutralizing Antibodies against HIV-1
Structure, 10:999-1011, 2002

PubMed Abstract: We report the 2.7 A resolution structure of a chimeric rhinovirus, MN-III-2, that displays part of the HIV-1 gp120 V3 loop and elicits HIV-neutralizing antibodies. The V3 loop insert is dominated by two type I beta turns. The structures of two adjacent tripeptides resemble those of analogous segments in three Fab/V3 loop peptide complexes. Although two of the three corresponding antibodies bind and neutralize MN-III-2 well, only one of the three can bind without significant rearrangement. These results suggest that the V3 loop insert: (1) can share some local conformational similarity to V3 loop sequences presented on different structural frameworks; (2) must be able to adopt multiple conformations, even in a relatively constrained environment; and (3) may mimic the conformational variability of the epitope on HIV-1, increasing the likelihood of eliciting appropriate neutralizing immune responses.

PubMed: 12121655
DOI: 10.1016/S0969-2126(02)00793-1

Experimental method

X-RAY DIFFRACTION (2.7 Å)