A Model of N-Terminal Cyclin T1 Based on FRET Experiments.pdfVIP

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A Model of N-Terminal Cyclin T1 Based on FRET Experiments.pdf

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A Model of N-Terminal Cyclin T1 Based on FRET Experiments.pdf

Journal of Theoretical Medicine, Vol. 6, No. 2, June 2005, 73–79 A model of N-terminal Cyclin T1 based on FRET experiments ` SERGIO PANTANO†k#, ALESSANDRO MARCELLO‡{#, ARIANNA SABO§, ALDO FERRARI{, VITTORIO PELLEGRINI{, FABIO BELTRAM{§, MAURO GIACCA‡{§* and PAOLO CARLONI†‡* †International School for Advanced Studies (ISAS) and INFM–DEMOCRITOS Modeling Center for Research in Atomistic Simulation, Via Beirut 2–4, 34014 Trieste, Italy ‡International Center for Genetic Engineering and Biotechnology (ICGEB), Padriciano 99, 34012 Trieste, Italy {National Enterprise for nanoScience and nanoTechnology–Istituto Nazionale di Fisica della Materia (NEST–INFM), Via della Faggiola 17, 56126 Pisa, Italy §Scuola Normale Superiore, Piazza dei Cavalieri 7, 56100 Pisa, Italy kVenetian Institute of Molecular Medicine (VIMM), Via Orus 2, 35129, Padua, Italy Human Cyclin T1 is the cyclin partner of kinase CDK9 in the positive transcription elongation factor b (P-TEFb). P-TEFb is recruited by Tat, the transactivator of the human immunodeﬁciency virus type 1 (HIV-1), to the viral promoter by direct interactions between Tat, Cyclin T1 and the cis-acting transactivation-responsive region (TAR) present at the 50 -end of each viral mRNA. At present, no structural data for Cyclin T1 are available. Here, we build a structural model of an N-terminus portion of Cyclin T1 (aa 27–263) based on the X-ray structure of Cyclin H. The model is compared with site directed mutagenesis d