Xianyang Fang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, USA
Jinbu Wang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, USA
Ina P O'Carroll, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Michelle Mitchell, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Xiaobing Zuo, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, USA
Yi Wang, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Ping Yu, Structual Bipphysics Laboratory, SAIC-Frederick, USA
Yu Liu, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, USA
Jason W Rausch, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Marzena A Dyba, Structual Bipphysics Laboratory, SAIC-Frederick, USA
Charles D Schwieters, Division of Computational Bioscience, Center for Inforamtional Technology, National Institutes of Health, USA
Soenke Seifert, X-ray Science Divsion, Argonne National Laborarory, USA
Randall E Winans, X-ray Science Divsion, Argonne National Laborarory, USA
Norman R Watts, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
Stephen J Stahl, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
Paul T Wingfield, Proteein Expression Laboratory, National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institute of Health, USA
R Andrew Byrd, Macromolecular NMR Section, Structural Biophysics Laboratory, Cente for Cancer Research, USA
Stuart F J Le Grice, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Alan Rein, RT Biochemestry Section, HIV Drug Resistance program, Center for Canser Researh, National Cancer Institute, National Center of Health, USA
Yun-Xing Wang, Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, HIV Drug Resistance Program, Center for Cancer Research, National Cancer Institute, National Institutes of Health, USA
Nuclear export of unspliced and singly spliced viral mRNA is a critical step in the HIV life cycle. The structural basis by which the virus selects its own mRNA among more abundant host cellular RNAs for export has been a mystery for more than 25 years. Here, we describe an unusual topological structure that the virus uses to recognize its own mRNA. The viral Rev response element (RRE) adopts an "A"-like structure in which the two legs constitute two tracks of binding sites for the viral Rev protein and position the two primary known Rev-binding sites ~55 Å apart, matching the distance between the two RNA-binding motifs in the Rev dimer. Both the legs of the "A" and the separation between them are required for optimal RRE function. This structure accounts for the specificity of Rev for the RRE and thus the specific recognition of the viral RNA.