Home
Resources
Publications
Insights From NMR Spectroscopy Into the Conformational Properties of Man-9 and Its Recognition by Two HIV Binding Proteins

Insights From NMR Spectroscopy Into the Conformational Properties of Man-9 and Its Recognition by Two HIV Binding Proteins

Syed Shahzad-Ul-Hussan, Mallika Sastry, Thomas Lemmin, Cinque Soto, Sandra Loesgen, Danielle A Scott, Jack R Davison, Katheryn Lohith, Robert O'Connor, Peter D Kwong, Carole A Bewley

Chembiochem. 2017 Apr 18;18(8):764-771.

PMID: 28166380

Abstract:

Man9 GlcNAc2 (Man-9) present at the surface of HIV makes up the binding sites of several HIV-neutralizing agents and the mammalian lectin DC-SIGN, which is involved in cellular immunity and trans-infections. We describe the conformational properties of Man-9 in its free state and when bound by the HIV entry-inhibitor protein microvirin (MVN), and define the minimum epitopes of both MVN and DC-SIGN by using NMR spectroscopy. To facilitate the implementation of 3D 13 C-edited spectra to deconvolute spectral overlap and to determine the solution structure of Man-9, we developed a robust expression system for the production of 13 C,15 N-labeled glycans in mammalian cells. The studies reveal that Man-9 interacts with HIV-binding proteins through distinct epitopes and adopts diverse conformations in the bound state. In combination with molecular dynamics simulations we observed receptor-bound conformations to be sampled by Man-9 in the free state, thus suggesting a conformational selection mechanism for diverse recognition.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP71246554	MAN-9 Glycan		71246-55-4	Price

As a specialist in analytical chemical Products, Alfa Chemistry offers consumers a wealth of raw materials and a full range of technologies and services.

QUICK LINKS

HEADQUARTERS

Tel:

Fax:

Email: