View source for 4rqs


==Crystal structure of fully glycosylated HIV-1 gp120 core bound to CD4 and 17b Fab==
<StructureSection load='4rqs' size='340' side='right'caption='[[4rqs]], [[Resolution|resolution]] 4.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4rqs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(isolate_YU2) Human immunodeficiency virus type 1 (isolate YU2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RQS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.493&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rqs OCA], [https://pdbe.org/4rqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rqs RCSB], [https://www.ebi.ac.uk/pdbsum/4rqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rqs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CD4_HUMAN CD4_HUMAN] Accessory protein for MHC class-II antigen/T-cell receptor interaction. May regulate T-cell activation. Induces the aggregation of lipid rafts.
<div style="background-color:#fffaf0;">
== 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<ref>PMID:25546301</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4rqs" style="background-color:#fffaf0;"></div>

==See Also==
*[[CD4 3D structures|CD4 3D structures]]
*[[Gp120 3D structures|Gp120 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kong L]]
[[Category: Kwong PD]]
[[Category: Wilson IA]]