| 저자(한글) |
Miyatake, H.,Sanjoh, A.,Murakami, T.,Murakami, H.,Matsuda, G.,Hagiwara, K.,Yokoyama, M.,Sato, H.,Miyamoto, Y.,Dohmae, N.,Aida, Y. |
| 초록 |
Viral protein R (Vpr) is an accessory gene product of human immunodeficiency virus type 1 (HIV-1) that plays multiple important roles associated with viral replication. Structural studies using NMR have revealed that Vpr consists of three alpha;-helices and contains flexible N- and C-termini. However, the molecular mechanisms associated with Vpr function have not been elucidated. To investigate Vpr multifunctionality, we performed an X-ray crystallographic study of Vpr complexes containing importin- alpha;, a known Vpr binding partner present in host cells. Elucidation of the crystal structure revealed that the flexible C-terminus changes its conformation to a twisted beta;-turn via an induced-fit mechanism, enabling binding to a minor nuclear localization signal (NLS) site of importin- alpha;. The Vpr C-terminus can also bind with major NLS sites of importin- alpha; in an extended conformation in different ways. These results, which represent the first reported crystallographic analysis of Vpr, demonstrate the multifunctional aspects that enable Vpr interaction with a variety of cellular proteins. |
