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Backbone 15 N relaxation analysis of the N‐terminal domain of the HTLV‐I capsid protein and comparison with the capsid protein of HIV‐1
Author(s) -
Cornilescu Claudia C.,
Bouamr Fadila,
Carter Carol,
Tjandra Nico
Publication year - 2003
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0235903
Subject(s) - capsid , heteronuclear molecule , retrovirus , chemistry , virology , biology , virus , nuclear magnetic resonance spectroscopy , stereochemistry
Human T‐cell leukemia virus type 1 (HTLV‐I) is an oncogenic retrovirus that exhibits specific tropism for human T‐cells. The capsid (CA) proteins of retroviruses share highly conserved secondary and tertiary structures. However, they can form quaternary structures (assembled cores) that are conical (e.g., the lentivirus subgroup, including HIV) or spherical (e.g., the oncovirus subgroup, including HTLV). The intrinsic features that drive these differences are not understood. So far, only structural studies have been used as a basis for comparison. Dynamics may play a role in particle formation. High‐resolution nuclear magnetic resonance (NMR) 15 N relaxation data ( T 1 , T 1ρ , and NOE) have been used to characterize the backbone dynamics of the N‐terminal domain (NTD) of the oncovirus HTLV‐I and to compare with the CA NTD of HIV‐1. Large variations in the 15 N heteronuclear NOEs and transversal relaxation rates for individual residues are consistent with the bundle RMSD of the previously calculated NMR structures. The β‐hairpin and CyP‐A loop exhibit different mobility in HTLV‐I and HIV‐1. The overall hydrodynamic property of the HTLV‐I capsid NTD is quite distinct from the HIV‐1.