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Default Flexible and Rigid Structures in HIV-1 p17 Matrix Protein Monitored by Relaxation and Amide Proton Exchange with NMR

Flexible and Rigid Structures in HIV-1 p17 Matrix Protein Monitored by Relaxation and Amide Proton Exchange with NMR

Publication date: Available online 26 December 2013
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author(s): Yuka Ohori , Honoka Okazaki , Satoru Watanabe , Naoya Tochio , Munehito Arai , Takanori Kigawa , Chiaki Nishimura

The HIV-1 p17 matrix protein is a multifunctional protein that interacts with other molecules including proteins and membranes. The dynamic structure between its folded and partially unfolded states can be critical for the recognition of interacting molecules. One of the most important roles of the p17 matrix protein is its localization to the plasma membrane with the Gag polyprotein. The myristyl group attached to the N-terminus on the p17 matrix protein functions as an anchor for binding to the plasma membrane. Biochemical studies revealed that two regions are important for its function: D14-L31 and V84-V88. Here, the dynamic structures of the p17 matrix protein were studied using NMR for relaxation and amide proton exchange experiments at the physiological pH of 7.0. The results revealed that the ?12-loop, which includes the 14–31 region, was relatively flexible, and that helix 4, including the 84–88 region, was the most protected helix in this protein. However, the residues in the ?34-loop near helix 4 had a low order parameter and high exchange rate of amide protons, indicating high flexibility. This region is probably flexible because this loop functions as a hinge for optimizing the interactions between helices 3 and 4. The C-terminal long region of K113-Y132 adopted a disordered structure. Furthermore, the C-terminal helix 5 appeared to be slightly destabilized due to the flexible C-terminal tail based on the order parameters. Thus, the dynamic structure of the p17 matrix protein may be related to its multiple functions.







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