Related ArticlesNMR insights into the conformational properties of Man-9 and its recognition by two HIV binding proteins.
Chembiochem. 2017 Feb 06;:
Authors: Shahzad-Ul-Hussan S, Sastry M, Lemmin T, Soto C, Loesgen S, Scott DA, Davison JR, O'Connor R, Kwong PD, Bewley CA
Abstract
Man9GlcNAc2 (Man-9) present at the surface of HIV constitutes the binding sites of several HIV neutralizing agents and mammalian lectin DC-SIGN that is involved in cellular immunity and trans-infections. We describe the conformational properties of Man-9 in free state and when bound by an HIV entry inhibitor protein and define the minimum epitopes of two HIV binding proteins using NMR spectroscopy. In this regard we developed a robust expression system for production of 13C,15N-labeled glycans in mammalian cells that facilitated the implementation of 3D 13C-edited spectra to deconvolute spectral overlap allowing for the solution structure determination of Man-9. The studies reveal that Man-9 interacts with HIV-binding proteins via distinct binding epitopes and adopts divergent conformations in the bound state. In combination with molecular dynamics we find that these receptor-bound conformations are sampled by Man-9 in the free state suggesting a mechanism for diverse recognition.
PMID: 28166380 [PubMed - as supplied by publisher]
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NMR insights into the conformational properties of Man-9 and its recognition by two HIV binding proteins.
Linear Mode
