TAILIEUCHUNG - Báo cáo khoa học: Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein

The capsid protein of HIV-1 (p24) (CA) forms the mature capsid of the human immunodeficiency virus. Capsid assembly involves hexamerization of the N-terminal domain and dimerization of the C-terminal domain of CA (CAC), and both domains constitute potential targets for anti-HIV therapy. | ỊFEBS Journal Structural mobility of the monomeric C-terminal domain of the HIV-1 capsid protein Luis A. Alcaraz Marta del Alamo2 Mauricio G. Mateu2 and Jose L. Neira1 3 1 Institute de Biologia Molecular y Celular Universidad MiguelHernandez Elche Alicante Spain 2 Centro de Biologia Molecular Severe Ochoa CSIC-UAM Universidad Autonoma de Madrid Spain 3 Biocomputation and Complex Systems Physics Institute Zaragoza Spain Keywords flexibility human immunodeficiency virus NMR structure Correspondence J. L. Neira Instituto de Biologia Molecular y Celular Edificio Torregaitan Universidad MiguelHernandez Avenida delFerrocarril s n 03202 Elche Alicante Spain Fax 34 966 658 758 Tel 34 966 658 459 E-mail jlneira@ These authors contributed equally to this work Received 4 February 2008 revised 22 April 2008 accepted 24 April 2008 doi The capsid protein of HIV-1 p24 CA forms the mature capsid of the human immunodeficiency virus. Capsid assembly involves hexamerization of the N-terminal domain and dimerization of the C-terminal domain of CA CAC and both domains constitute potential targets for anti-HIV therapy. CAC homodimerization occurs mainly through its second helix and it is abolished when its sole tryptophan is mutated to alanine. This mutant CACW40A resembles a transient monomeric intermediate formed during dimerization. Its tertiary structure is similar to that of the subunits in the dimeric non-mutated CAC but the segment corresponding to the second helix samples different conformations. The present study comprises a comprehensive examination of the CACW40A internal dynamics. The results obtained with movements sampling a wide time regime from pico-to milliseconds demonstrate the high flexibility of the whole monomeric protein. The conformational exchange phenomena on the micro-to-milli-second time scale suggest a role for internal motions in the monomermonomer interactions and thus flexibility of the polypeptide chain is likely to

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