User:David Ryskamp/Sandbox1: Difference between revisions
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== Structure == | == Structure == | ||
<StructureSection load='1cvj' size='340' side='right' caption='PABP' scene='78/782614/Structure_scene_color_scheme/1'> | <StructureSection load='1cvj' size='340' side='right' caption='PABP' scene='78/782614/Structure_scene_color_scheme/1'> __NoTOC__ | ||
The crystal structure PABP was derived from X-ray Diffraction at 2.6Å (R-value: 23%). The subunits of PABP, RRM1 and RRM2, are examined in this article as the ''in vivo'' form seen in biological assembly 1 (via PDB). The protein has a homopolymeric structure, containing four RNA recognition motifs (RRMs), which are conserved. <ref name="Structure and Function">Kühn, Uwe and Elmar, Wahle. “Structure and Function of Poly(a) Binding Proteins.” Bba - Gene Structure & Expression, vol. 1678, no. 2/3, 2004. </ref> <scene name='78/782616/Rrm1_only/2'>RRM1</scene> and <scene name='78/782616/Rrm2_only/2'>RRM2</scene> are N-terminal domains that are connected by a <scene name='78/782616/Linker/3'>linker</scene>.<ref name="Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein">Deo, Rahul C, et al. “Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein.” Cell 98:6. (1999) 835-845. Print. </ref> Opposed to their counterparts, RRM3 and RRM4 bind Poly (A) RNA less tightly than RRM1 and RRM2.<ref name="Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein">Deo, Rahul C, et al. “Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein.” Cell 98:6. (1999) 835-845. Print. </ref> | The crystal structure PABP was derived from X-ray Diffraction at 2.6Å (R-value: 23%). The subunits of PABP, RRM1 and RRM2, are examined in this article as the ''in vivo'' form seen in biological assembly 1 (via PDB). The protein has a homopolymeric structure, containing four RNA recognition motifs (RRMs), which are conserved. <ref name="Structure and Function">Kühn, Uwe and Elmar, Wahle. “Structure and Function of Poly(a) Binding Proteins.” Bba - Gene Structure & Expression, vol. 1678, no. 2/3, 2004. </ref> <scene name='78/782616/Rrm1_only/2'>RRM1</scene> and <scene name='78/782616/Rrm2_only/2'>RRM2</scene> are N-terminal domains that are connected by a <scene name='78/782616/Linker/3'>linker</scene>.<ref name="Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein">Deo, Rahul C, et al. “Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein.” Cell 98:6. (1999) 835-845. Print. </ref> Opposed to their counterparts, RRM3 and RRM4 bind Poly (A) RNA less tightly than RRM1 and RRM2.<ref name="Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein">Deo, Rahul C, et al. “Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein.” Cell 98:6. (1999) 835-845. Print. </ref> | ||
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In more complex eukaryotic organisms, PABP indirectly stimulates translation via [https://en.wikipedia.org/wiki/PAIP1 PAIP-1] (PABP interacting protein). A higher presence of PAIP-1 increases the rate of translation initiation, indicating another way to “close the loop.”¹ | In more complex eukaryotic organisms, PABP indirectly stimulates translation via [https://en.wikipedia.org/wiki/PAIP1 PAIP-1] (PABP interacting protein). A higher presence of PAIP-1 increases the rate of translation initiation, indicating another way to “close the loop.”¹ | ||
</StructureSection> | </StructureSection> | ||
==Disease and Medical Relevance== | ==Disease and Medical Relevance== | ||
