Sandbox WWC8: Difference between revisions

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== Structural Features ==

The globular NP protein is rich in arginine, serine, and glycine residues. The abundance of arginine residues gives the protein a net positive charge at pH 7. With a predicted pI of 9.3, NP is mainly composed of basic residues, except for a tail domain of the 30 C-terminal residues, which are acidic. The C-tail domain has a pI of 3.7 <ref>1</ref>. The NP is a homo 3-mer - A3 with 499 amino acid residues encoded by the Influenza A RNA segment 5.Each homomer provides a binding site for the viral RNA script <ref>1</ref>.

The globular NP protein is rich in arginine, serine, and glycine residues. The abundance of arginine residues gives the protein a net positive charge at pH 7. With a predicted pI of 9.3, NP is mainly composed of basic residues, except for a tail domain of the 30 C-terminal residues, which are acidic. The C-tail domain has a pI of 3.7 <ref>1</ref>. The NP is a homo 3-mer - A3 with 499 amino acid residues encoded by the Influenza A RNA segment 5. Each homomer provides a binding site for the viral RNA script <ref>1</ref>.

The homomers fold into a crescent shape with a head and a body domain, where the grove between the two domains hosts the ssRNA binding site on the outer surface of the homomer <ref>1</ref><ref>2</ref>. For the formation of RNPs, the NP needs to form a coordinated aggregate of three NPs through a process called homo-oligomerization <ref>2</ref><ref>3</ref>. The C-tail loop, marked in pink in the image below, is critical for this function. Residues 408-419, located at the back of the NP between head and tail domain, form a loop that is the basis of the interface between neighboring NPs. The C-tail loop interlock with the loop binding cavity in the neighboring NP and form a tight binding interaction, featuring both hydrophobic and hydrophilic residues, that keeps the homo 3-mer together. The NP oligomer conformation is especially stabilized by a salt bridge between Arg 416 in the loop and Glu339 in the adjacent NP <ref>2</ref>.

Sandbox WWC8: Difference between revisions

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 == Structural Features ==
-The globular NP protein is rich in arginine, serine, and glycine residues. The abundance of arginine residues gives the protein a net positive charge at pH 7. With a predicted pI of 9.3, NP is mainly composed of basic residues, except for a tail domain of the 30 C-terminal residues, which are acidic. The C-tail domain has a pI of 3.7 <ref>1</ref>. The NP is a homo 3-mer - A3 with 499 amino acid residues encoded by the Influenza A RNA segment 5.Each homomer provides a binding site for the viral RNA script <ref>1</ref>.
+The globular NP protein is rich in arginine, serine, and glycine residues. The abundance of arginine residues gives the protein a net positive charge at pH 7. With a predicted pI of 9.3, NP is mainly composed of basic residues, except for a tail domain of the 30 C-terminal residues, which are acidic. The C-tail domain has a pI of 3.7 <ref>1</ref>. The NP is a homo 3-mer - A3 with 499 amino acid residues encoded by the Influenza A RNA segment 5. Each homomer provides a binding site for the viral RNA script <ref>1</ref>.
 The homomers fold into a crescent shape with a head and a body domain, where the grove between the two domains hosts the ssRNA binding site on the outer surface of the homomer <ref>1</ref><ref>2</ref>. For the formation of RNPs, the NP needs to form a coordinated aggregate of three NPs through a process called homo-oligomerization <ref>2</ref><ref>3</ref>. The C-tail loop, marked in pink in the image below, is critical for this function. Residues 408-419, located at the back of the NP between head and tail domain, form a loop that is the basis of the interface between neighboring NPs. The C-tail loop interlock with the loop binding cavity in the neighboring NP and form a tight binding interaction, featuring both hydrophobic and hydrophilic residues, that keeps the homo 3-mer together. The NP oligomer conformation is especially stabilized by a salt bridge between Arg 416 in the loop and Glu339 in the adjacent NP <ref>2</ref>.