User:Ben Dawson/Sandbox1: Difference between revisions

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== Background ==
== Background ==
The Human Poly-A Binding Protein (PABP) is a mRNA binding protein that binds to the 3’ Poly-A tail on mRNA. Through extensive Adenosine recognition by the RNA REcognition Motifs (RRMs) of PABP, the protein is involved in three main functions: recognition of the 3’ Poly-A tail, mRNA stabilization, and eukaryotic translation initiation. The contributions of controlling gene expression via different families of PABPs is not yet fully understood. PABP families are divided into nuclear and cytoplasmic.5 PABP1, which is predominantly cytoplasmic, is often referred to as PABP because it is the only form of PABP that has been extensively studied in its role with mRNA translation and stability.5  
The Human Poly-A Binding Protein (PABP) is a mRNA binding protein that binds to the 3’ Poly-A tail of mRNA prior to translation. Through extensive Adenosine recognition by the RNA Recognition Motifs (RRMs) of PABP, the protein is involved in three main functions: recognition of the 3’ Poly-A tail, mRNA stabilization, and, even further, eukaryotic translation initiation. The contributions of controlling gene expression via different families of PABPs is not yet fully understood. PABP families are divided into nuclear and cytoplasmic.5 PABP1, which is predominantly cytoplasmic, is often referred to as PABP because it is the only form of PABP that has been extensively studied in its role with mRNA translation and stability.5  




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The crystall structure was derived from X-ray Diffraction at 2.6Å (R-value: 23%). It is comprised of four RNA recognition motifs (RRMs), which are highly conserved RNA-binding domains.¹ The RRM in PABP is found in over two hundred families of proteins across species, indicating that it is ancient.¹ RRM1 and 2 are examined in this article.
The crystall structure was derived from X-ray Diffraction at 2.6Å (R-value: 23%). It is comprised of four RNA recognition motifs (RRMs), which are highly conserved RNA-binding domains.¹ The RRM in PABP is found in over two hundred families of proteins across species, indicating that it is ancient.¹ RRM1 and 2 are examined in this article.
Each RRM has four-stranded antiparallel beta sheet and two helices.¹ Recent studies have shown that mRNA binding is due to the presence of the beta-sheet surfaces.²  (image- trough). The beta-sheet flooring present in PABP interacts with the 3’ mRNA tail via a combination of van der Waals, aromatic stacking, and Hydrogen bonding. Through these interactions, PABP binds to 3’ poly-adenosine tail with a KD of 2-7 nM.5  The structural elements highlighted consist of the RRM1/2 subunits, the linker domain, and the Poly-A mRNA binding trough.  
Each RRM has a four-stranded antiparallel beta sheet and two alpha helices.¹ mRNA poly-adenosine recognition is due to the presence of the conserved residues within the beta-sheet surface², which forms a <scene name='78/782616/Trough2/1'>trough</scene>-like pocket for the mRNA to bind . The beta-sheet flooring present in PABP interacts with the 3’ mRNA tail via a combination of van der Waals, aromatic stacking, and Hydrogen bonding. Through these interactions, PABP binds to 3’ poly-adenosine tail with a KD of 2-7 nM.5  The structural elements highlighted consist of the RRM1/2 subunits, the linker domain, and the Poly-A mRNA binding trough.  




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