Sandbox Reserved 1654: Difference between revisions

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</StructureSection>

RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.

RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other:

***RRM1 has ~~an extended beta-sheet surface resulting from the insertion of two conserved,~~ anti-parallel beta strands between the alpha helix and the beta4 strand.

***RRM1 has anti-parallel beta strands between the alpha helix and the beta4 strand.

***~~Following RRM1, the initial region of the~~ interdomain linker ~~in CPEB1 adopts~~ a ~~short~~ helical turn that interacts with residues of the N-terminal extension ~~as well as~~ with RRM2.

***The interdomain linker takes a helical turn that interacts with residues of the N-terminal extension and with RRM2.

***Trp331 ~~makes key interactions to position~~ RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. ***After the helical turn, the interdomain linker folds in a beta strand ~~that runs~~ anti-parallel to the beta2 strand (RRM2) ~~and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet~~. ~~Therefore, the~~ interdomain linker ~~acts as~~ a ~~hinge to fix~~ the relative orientation of the two RRMs.

***<scene name='86/868187/Rmm/1'>Trp331</scene> positions RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2.

***After the helical turn, the interdomain linker folds in a beta strand which is anti-parallel to the beta2 strand (RRM2). The interdomain linker is therefore a kind of joint for the relative orientation of the two RRMs.

== Function ==

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@@ Line 20: / Line 20: @@
 <StructureSection load='2MKK' size='350' side='right' caption='RNA binding to RRM' scene=''>
 </StructureSection>
-RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other.
+RRMs are necessary and sufficient for the CPE sequence recognition on RNA. They bind to RNA with high affinity and allow the RNA to take the good position. RRM1 binds to the four first RNA nucleotides (UUUU) and RRM2 binds to the 3' adenine of CPE. The two RRMs take a V-shaped conformation, facing to each other:
-***RRM1 has an extended beta-sheet surface resulting from the insertion of two conserved, anti-parallel beta strands between the alpha helix and the beta4 strand.
+***RRM1 has anti-parallel beta strands between the alpha helix and the beta4 strand.
-***Following RRM1, the initial region of the interdomain linker in CPEB1 adopts a short helical turn that interacts with residues of the N-terminal extension as well as with RRM2.
+***The interdomain linker takes a helical turn that interacts with residues of the N-terminal extension and with RRM2.
-***Trp331 makes key interactions to position RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2. ***After the helical turn, the interdomain linker folds in a beta strand that runs anti-parallel to the beta2 strand (RRM2) and packs against the alpha1 helix of RRM2. Finally, the interdomain linker runs across the RRM2 beta sheet. Therefore, the interdomain linker acts as a hinge to fix the relative orientation of the two RRMs.
+***<scene name='86/868187/Rmm/1'>Trp331</scene> positions RRM2 relative to RRM1 by inserting its indole ring between the beta sheet and alpha1 helix of RRM2.
+***After the helical turn, the interdomain linker folds in a beta strand which is anti-parallel to the beta2 strand (RRM2). The interdomain linker is therefore a kind of joint for the relative orientation of the two RRMs.
 == Function ==