6B3U

Solution Structure of HIV-1 GP41 Transmembrane Domain in Bicelles

Summary for 6B3U

• Entry DOI: 10.2210/pdb6b3u/pdb
• NMR Information: BMRB: 30349
• Descriptor: HIV-1 GP41 Transmembrane Domain (1 entity in total)
• Functional Keywords: hiv-1, transmembrane domain, gp41, solution structure, residual dipolar couplings, membrane protein
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 1
• Total formula weight: 4650.60

Authors

Chiliveri, S.C.,Louis, J.M.,Ghirlando, R.,Baber, J.L.,Bax, A. (deposition date: 2017-09-24, release date: 2018-01-24, Last modification date: 2024-05-15)

Primary citation

Chiliveri, S.C.,Louis, J.M.,Ghirlando, R.,Baber, J.L.,Bax, A.
Tilted, Uninterrupted, Monomeric HIV-1 gp41 Transmembrane Helix from Residual Dipolar Couplings.
J. Am. Chem. Soc., 140:34-37, 2018

PubMed Abstract: Cryo-electron microscopy and X-ray crystallography have shown that the pre- and postfusion states of the HIV-1 gp41 viral coat protein, although very different from one another, each adopt C symmetric structures. A stable homotrimeric structure for the transmembrane domain (TM) also was modeled and supported by experimental data. For a C symmetric structure, alignment in an anisotropic medium must be axially symmetric, with the unique axis of the alignment tensor coinciding with the C axis. However, NMR residual dipolar couplings (RDCs) measured under three different alignment conditions were found to be incompatible with C symmetry. Subsequent measurements by paramagnetic relaxation enhancement, analytical ultracentrifugation, and DEER EPR, indicate that the transmembrane domain is monomeric. N NMR relaxation data and RDCs show that TM is highly ordered and uninterrupted for a total length of 32 residues, extending well into the membrane proximal external region.

PubMed: 29277995
DOI: 10.1021/jacs.7b10245

Experimental method

SOLUTION NMR