Prp24: Difference between revisions

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===Structural Models===

A recent study <ref name="Bae"/> examined the structure of the N-terminal domain and first three RRMs of Prp24 by X-ray crystallography (green link back to main structure?). The resultant structure showed Prp24 as an octameric protein, 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 (green link back to main structure?). The resultant structure showed Prp24 as an octameric protein, 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"/>.

== Functional Interactions ==

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@@ Line 38: / Line 38: @@
 ===Structural Models===
-A recent study <ref name="Bae"/> examined the structure of the N-terminal domain and first three RRMs of Prp24 by X-ray crystallography (green link back to main structure?).  The resultant structure showed Prp24 as an octameric protein, 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 (green link back to main structure?).  The resultant structure showed Prp24 as an octameric protein, 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"/>.
 == Functional Interactions ==