Prp24: Difference between revisions

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===Structural Models===

A recent study <ref name="Bae"/> examined the structure of <scene name='Sandbox_Reserved_340/2ghp/4'>the N-terminal domain and first three RRMs</scene>of Prp24 by X-ray crystallography ~~(green link back to main structure?)~~. The resultant structure showed Prp24 as an <scene name='Sandbox_Reserved_340/2ghp/5'>octameric protein</scene>, consisting of eight chains arranged in two nearly symmetrical tetramers<ref name="Bae"/>. This was the first suggested that Prp24 functioned as an multimer, so it is unclear what the significance of this result is <ref name="Bae"/>. Their crystal structure also showed extensive interactions between both RRM 1 and 2 ~~(green link)~~ and RRM 2 and 3 ~~(green link)~~, and NMR analysis of protein fragments containing either RRMs 1 and 2 or RRMs 2 and 3 showed that these interactions existed in solution as well<ref name="Bae"/>. Interestingly, these interactions seemed to block the proposed U6 binding sites of RRM 1 and 2; NMR analysis of the RRM 1 and 2 protein fragment with an RNA oligomer containing the U6 sequences thought to bind the RRMs showed a largely canonical interaction of the RNA with the RRMs, suggesting that Prp24 may undergo conformational changes in the binding of U6<ref name="Bae"/>.

A recent study <ref name="Bae"/> examined the structure of <scene name='Sandbox_Reserved_340/2ghp/4'>the N-terminal domain and first three RRMs</scene>of Prp24 by X-ray crystallography. The resultant structure showed Prp24 as an <scene name='Sandbox_Reserved_340/2ghp/5'>octameric protein</scene>, consisting of eight chains arranged in two nearly symmetrical tetramers<ref name="Bae"/>. This was the first suggested that Prp24 functioned as an multimer, so it is unclear what the significance of this result is <ref name="Bae"/>. Their crystal structure also showed extensive interactions between both <scene name='Sandbox_Reserved_340/2ghp/9'>RRM 1 and 2</scene> and <scene name='Sandbox_Reserved_340/2ghp/10'>RRM 2 and 3</scene>, and NMR analysis of protein fragments containing either RRMs 1 and 2 or RRMs 2 and 3 showed that these interactions existed in solution as well<ref name="Bae"/>. Interestingly, these interactions seemed to block the proposed U6 binding sites of RRM 1 and 2; NMR analysis of the RRM 1 and 2 protein fragment with an RNA oligomer containing the U6 sequences thought to bind the RRMs showed a largely canonical interaction of the RNA with the RRMs, suggesting that Prp24 may undergo conformational changes in the binding of U6<ref name="Bae"/>.

== Functional Interactions ==

Prp24 is part of the normal U6 snRNP, along with seven Lsm proteins <ref name="Brow review"/>. After interaction with the U4 snRNP to form the U4/U6 di-snRNP, Prp24 departs from the di-snRNP before the addition of U5 to form the tri-snRNP U4/U6.U5 <ref name="Brow review"/>. Through many studies, it has been shown that Prp24 interacts extensively with specific sites on U6, as well with the Lsm protein ring on the 3' terminal end of the U6 snRNA.

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@@ Line 38: / Line 38: @@
 ===Structural Models===
-A recent study <ref name="Bae"/> examined the structure of <scene name='Sandbox_Reserved_340/2ghp/4'>the N-terminal domain and first three RRMs</scene>of Prp24 by X-ray crystallography (green link back to main structure?).  The resultant structure showed Prp24 as an <scene name='Sandbox_Reserved_340/2ghp/5'>octameric protein</scene>, consisting of eight chains arranged in two nearly symmetrical tetramers<ref name="Bae"/>.  This was the first suggested that Prp24 functioned as an multimer, so it is unclear what the significance of this result is <ref name="Bae"/>.  Their crystal structure also showed extensive interactions between both RRM 1 and 2 (green link) and RRM 2 and 3 (green link), and NMR analysis of protein fragments containing either RRMs 1 and 2 or RRMs 2 and 3 showed that these interactions existed in solution as well<ref name="Bae"/>.  Interestingly, these interactions seemed to block the proposed U6 binding sites of RRM 1 and 2; NMR analysis of the RRM 1 and 2 protein fragment with an RNA oligomer containing the U6 sequences thought to bind the RRMs showed a largely canonical interaction of the RNA with the RRMs, suggesting that Prp24 may undergo conformational changes in the binding of U6<ref name="Bae"/>.
+A recent study <ref name="Bae"/> examined the structure of <scene name='Sandbox_Reserved_340/2ghp/4'>the N-terminal domain and first three RRMs</scene>of Prp24 by X-ray crystallography.  The resultant structure showed Prp24 as an <scene name='Sandbox_Reserved_340/2ghp/5'>octameric protein</scene>, consisting of eight chains arranged in two nearly symmetrical tetramers<ref name="Bae"/>.  This was the first suggested that Prp24 functioned as an multimer, so it is unclear what the significance of this result is <ref name="Bae"/>.  Their crystal structure also showed extensive interactions between both <scene name='Sandbox_Reserved_340/2ghp/9'>RRM 1 and 2</scene> and <scene name='Sandbox_Reserved_340/2ghp/10'>RRM 2 and 3</scene>, and NMR analysis of protein fragments containing either RRMs 1 and 2 or RRMs 2 and 3 showed that these interactions existed in solution as well<ref name="Bae"/>.  Interestingly, these interactions seemed to block the proposed U6 binding sites of RRM 1 and 2; NMR analysis of the RRM 1 and 2 protein fragment with an RNA oligomer containing the U6 sequences thought to bind the RRMs showed a largely canonical interaction of the RNA with the RRMs, suggesting that Prp24 may undergo conformational changes in the binding of U6<ref name="Bae"/>.
 == Functional Interactions ==
-<Structure load='2ghp' size='300' frame='true' align='right' caption='Insert caption here' scene='Sandbox_Reserved_340/2ghp/3'/>
+<Structure load='2ghp' size='300' frame='true' align='right' caption='' scene='Sandbox_Reserved_340/2ghp/3'/>
 Prp24 is part of the normal U6 snRNP, along with seven Lsm proteins <ref name="Brow review"/>.  After interaction with the U4 snRNP to form the U4/U6 di-snRNP, Prp24 departs from the di-snRNP before the addition of U5 to form the tri-snRNP U4/U6.U5 <ref name="Brow review"/>.  Through many studies, it has been shown that Prp24 interacts extensively with specific sites on U6, as well with the Lsm protein ring on the 3' terminal end of the U6 snRNA.