1o0p: Difference between revisions

Line 4:

==Overview==

The essential splicing factors SF1 and U2AF play an important role in the, recognition of the pre-mRNA 3' splice site during early spliceosome, assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65), complexed to an N-terminal peptide of SF1 reveals an extended negatively, charged helix A and an additional helix C. Helix C shields the potential, RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It, inserts a conserved tryptophan into a hydrophobic pocket between helices A, and B in a way that strikingly resembles part of the molecular interface, in the U2AF heterodimer. This molecular recognition establishes a paradigm, for protein binding by a subfamily of noncanonical RRMs.

The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.

==About this Structure==

Line 24:

[[Category: non-canonical rna recognition motif]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 16~~:31:47 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:15 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 4: / Line 4: @@
 ==Overview==
-The essential splicing factors SF1 and U2AF play an important role in the, recognition of the pre-mRNA 3' splice site during early spliceosome, assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65), complexed to an N-terminal peptide of SF1 reveals an extended negatively, charged helix A and an additional helix C. Helix C shields the potential, RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It, inserts a conserved tryptophan into a hydrophobic pocket between helices A, and B in a way that strikingly resembles part of the molecular interface, in the U2AF heterodimer. This molecular recognition establishes a paradigm, for protein binding by a subfamily of noncanonical RRMs.
+The essential splicing factors SF1 and U2AF play an important role in the recognition of the pre-mRNA 3' splice site during early spliceosome assembly. The structure of the C-terminal RRM (RRM3) of human U2AF(65) complexed to an N-terminal peptide of SF1 reveals an extended negatively charged helix A and an additional helix C. Helix C shields the potential RNA binding surface. SF1 binds to the opposite, helical face of RRM3. It inserts a conserved tryptophan into a hydrophobic pocket between helices A and B in a way that strikingly resembles part of the molecular interface in the U2AF heterodimer. This molecular recognition establishes a paradigm for protein binding by a subfamily of noncanonical RRMs.
 ==About this Structure==
@@ Line 24: / Line 24: @@
 [[Category: non-canonical rna recognition motif]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:31:47 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:12:15 2008''