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5FUU

Ectodomain of cleaved wild type JR-FL EnvdCT trimer in complex with PGT151 Fab

This is a non-PDB format compatible entry.
Summary for 5FUU
Entry DOI10.2210/pdb5fuu/pdb
EMDB information3308
DescriptorHIV-1 ENVELOPE GLYCOPROTEIN GP160, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (16 entities in total)
Functional Keywordsviral protein, hiv-1, env, pgt151, broadly neutralizing antibody
Biological sourceHUMAN IMMUNODEFICIENCY VIRUS 1
More
Total number of polymer chains10
Total formula weight353076.17
Authors
Lee, J.H.,Ward, A.B. (deposition date: 2016-01-29, release date: 2016-03-09, Last modification date: 2024-10-23)
Primary citationLee, J.H.,Ozorowski, G.,Ward, A.B.
Cryo-Em Structure of a Native, Fully Glycosylated and Cleaved HIV-1 Envelope Trimer
Science, 351:1043-, 2016
Cited by
PubMed Abstract: The envelope glycoprotein trimer (Env) on the surface of HIV-1 recognizes CD4(+) T cells and mediates viral entry. During this process, Env undergoes substantial conformational rearrangements, making it difficult to study in its native state. Soluble stabilized trimers have provided valuable insights into the Env structure, but they lack the hydrophobic membrane proximal external region (MPER, an important target of broadly neutralizing antibodies), the transmembrane domain, and the cytoplasmic tail. Here we present (i) a cryogenic electron microscopy (cryo-EM) structure of a clade B virus Env, which lacks only the cytoplasmic tail and is stabilized by the broadly neutralizing antibody PGT151, at a resolution of 4.2 angstroms and (ii) a reconstruction of this form of Env in complex with PGT151 and MPER-targeting antibody 10E8 at a resolution of 8.8 angstroms. These structures provide new insights into the wild-type Env structure.
PubMed: 26941313
DOI: 10.1126/SCIENCE.AAD2450
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.19 Å)
Structure validation

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건을2026-02-04부터공개중

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