Structural Characterization of Membrane-Bound Human Immunodeficiency Virus-1 Gag Matrix with Neutron Reflectometry

Published

May 1, 2017

Author(s)

Rebecca Eells, Marilia Barros, Kerry M. Scott, Ioannis Karageorgos, Frank Heinrich, Mathias Loesche

Abstract

The structural characterization of peripheral membrane proteins represents a tremendous challenge in structural biology due to their transient interaction with the membrane and the potential multitude of protein conformations during this interaction. Neutron reflectometry is uniquely suited to address this problem, because of its ability to structurally characterize biological model systems non-destructively and under biomimetic conditions that retain full protein model systems non-destructively and under biomimetic conditions that retain full protein functionality. Being sensitive to only the membrane-bound fraction of a water-soluble peripheral protein, neutron reflectometry obtains a low-resolution average structure of the protein-membrane complex that is further refined using integrative modeling strategies. Here we review the current technological state of biological neutron reflectometry exemplified by a detailed report on the structure determination of myristoylated HIV-1 Gag matrix associated with phosphoserine-containing model membranes. We found that HIV-2 Gag matrix is able to adopt different configurations at the membrane in a pH-dependent manner and that the myristate group orients the protein in a way that is a conducive to PIP₂-binding.

Citation

Biointerphases

Volume

12

Issue

2

Pub Type

Journals

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Keywords

neutron reflectometry, peripheral membrane proteins

Citation

Eells, R. , Barros, M. , Scott, K. , Karageorgos, I. , Heinrich, F. and Loesche, M. (2017), Structural Characterization of Membrane-Bound Human Immunodeficiency Virus-1 Gag Matrix with Neutron Reflectometry, Biointerphases, [online], https://tsapps.nist.gov/publication/get_pdf.cfm?pub_id=923113 (Accessed April 19, 2024)