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SUMMARY:The mechanism of retroviral DNA integration through X-ray structur
 es of its key intermediates 
DTSTART:20110202T170000
DTSTAMP:20260919T215359Z
UID:da522c51e2bcf079fdea1c658444b68a7e465f7a076aea0adf5d5c42
CATEGORIES:Conferences - Seminars
DESCRIPTION:Peter Cherepanov\, PhD\nTo establish successful infection\, a 
 retrovirus must insert a DNA replica of its genome into host cell chromoso
 mal DNA. This process is orchestrated by integrase (IN)\, a viral enzyme t
 hat belongs to the DDE(D) nucleotidyltransferase/transposase superfamily. 
 Following reverse transcription\, IN catalyses two essential reactions\, 3
 ´-end processing and strand transfer\, acting upon both ends of the linea
 r viral DNA. To carry out these functions IN synapses the viral DNA ends f
 orming a highly stable nucleoprotein complex\, termed intasome. Upon nucle
 ar entry\, the intasome engages host chromosomal DNA within a target captu
 re complex to execute strand transfer\, irreversibly joining the viral and
  cellular DNA molecules. \nWe reported a crystal structure of the prototyp
 e foamy virus intasome comprising a tetramer of IN assembled on processed 
 viral DNA ends (Hare et al.\, Nature\, 2010\, 464:232-6). The structure re
 vealed for the first time a fully assembled IN active site\, engaged with 
 the 3´ end of the viral DNA and a pair of metal cations. More recently de
 termined crystal structures of the viral nucleoprotein complex prior to 3
 ´-processing (in preparation for publication) and of the intasome bound t
 o target DNA within the pre-strand transfer and post-catalytic intermediat
 es (Maertens et al.\, Nature\, 2010\, 468:326-329). Collectively\, these s
 tructures illustrate all key stages of the retroviral DNA integration proc
 ess\, elucidate the mechanics of the IN active site and moreover provide a
  framework for the design of INs with altered target sequences.
LOCATION:SV 1717 A
STATUS:CONFIRMED
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