Nuclear polyadenylated RNA-binding protein: Difference between revisions
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=Structure= | =Structure= | ||
==General Features== | ==General Features== | ||
Hrp1 is a single-stranded [https://en.wikipedia.org/wiki/RNA-binding_protein RNA-binding protein] composed of two RNP-type [https://en.wikipedia.org/wiki/RNA_recognition_motif RNA-binding domains (RBDs)] arranged in tandem with a typical ßαßßαß architecture <ref name="GM3H"/>. The two RBDs have similar topolgies, both containing a central [https://en.wikipedia.org/wiki/Beta_sheet antiparallel] four-stranded <scene name='78/783765/Beta_sheet/1'>ß-sheet</scene> with two [https://en.wikipedia.org/wiki/Alpha_helix α-helices] running across one face <ref name="GM3H"/>. The β-strands of each βαβ domain are linked via hydrogen bonding between conserved residues, <scene name='78/783765/L166_g201/ | Hrp1 is a single-stranded [https://en.wikipedia.org/wiki/RNA-binding_protein RNA-binding protein] composed of two RNP-type [https://en.wikipedia.org/wiki/RNA_recognition_motif RNA-binding domains (RBDs)] arranged in tandem with a typical ßαßßαß architecture <ref name="GM3H"/>. The two RBDs have similar topolgies, both containing a central [https://en.wikipedia.org/wiki/Beta_sheet antiparallel] four-stranded <scene name='78/783765/Beta_sheet/1'>ß-sheet</scene> with two [https://en.wikipedia.org/wiki/Alpha_helix α-helices] running across one face <ref name="GM3H"/>. The β-strands of each βαβ domain are linked via hydrogen bonding between conserved residues, <scene name='78/783765/L166_g201/3'>Leu166 and Gly201</scene>. The two RBDs associate to form a deep and positively charged <scene name='78/781960/Hrp1-rna_interface_surface/2'>cleft</scene>, which constitutes the binding site for the RNA molecule <ref name="GM3H"/>. | ||
==Hrp1-RNA Interactions== | ==Hrp1-RNA Interactions== | ||
