4rqs

Crystal structure of fully glycosylated HIV-1 gp120 core bound to CD4 and 17b Fab

spinqualitylabelsall models 4rqs, resolution 4.49Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rqs is a 4 chain structure with sequence from Homo sapiens and Human immunodeficiency virus type 1 (isolate YU2). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 4.493Å Ligands: BMA, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CD4_HUMAN Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts. Publication Abstract from PubMed The crystal structure of a fully glycosylated HIV-1 gp120 core in complex with CD4 receptor and Fab 17b at 4.5 A resolution reveals 9 of the 15 N-linked glycans of core gp120 to be partially ordered. The glycan at position Asn262 had the most extensive and well-ordered electron density, and a GlcNAc2 Man7 was modeled. The GlcNAc stem of this glycan is largely buried in a cleft in gp120, suggesting a role in gp120 folding and stability. Its arms interact with the stems of neighboring glycans from the oligomannose patch, which is a major target for broadly neutralizing antibodies. This article is protected by copyright. All rights reserved. Crystal structure of a fully glycosylated HIV-1 gp120 core reveals a stabilizing role for the glycan at Asn262.,Kong L, Wilson IA, Kwong PD Proteins. 2014 Dec 26. doi: 10.1002/prot.24747. PMID:25546301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CD4 3D structures Gp120 3D structures

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