RiAFP: Difference between revisions

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== Overall Structure ==
== Overall Structure ==
The crystallographic structure of RiAFP was defined recently<ref>DOI 10.1074/jbc.M113.450973</ref>. It reveals a new β-solenoid architecture that forms <scene name='60/607864/Beta_sheets/1'>β-sandwich</scene> of <scene name='60/607864/Beta_sheets_colored/1'>two parallel 6 and 7 stranded-sheets</scene>  of remarkable regularity. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming <scene name='60/607864/Beta_sheets_capping/2'>capping structures</scene>. These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation.
The crystallographic structure of RiAFP was defined recently<ref>DOI 10.1074/jbc.M113.450973</ref>. It reveals a new β-solenoid architecture that forms <scene name='60/607864/Beta_sheets/1'>β-sandwich</scene> of <scene name='60/607864/Beta_sheets_colored/1'>two parallel 6 and 7 stranded-sheets</scene>  of remarkable regularity. The β-sheets lie on top of each other with the upper and lower strands parallel but in the opposite orientation. Two ends deviate from β helix regularity by forming <scene name='60/607864/Beta_sheets_capping/2'>capping structures</scene>. These capping structures help to prevent end-to-end associations that would spoil the solubility of RiAFP and lead to oligomerization and aggregation.
The three residues in β-strand 11 at the C terminus <scene name='60/607864/Gln110_gln112_ile114/1'>(Gln110, Gln112, and Ile114)</scene> that are too bulky to be accommodated into the core may also contribute to the capping structure to prevent amyloid-like polymerization.
== Function ==
== Function ==
<scene name='60/607864/Riafp/1'>TextToBeDisplayed</scene>
<scene name='60/607864/Riafp/1'>TextToBeDisplayed</scene>
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This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
The three residues in �-strand 11 at the C terminus <scene name='60/607864/Three_capping_residues/2'>(Gln110, Gln112, and Ile114)</scene> that are too bulky to be accommodated into the core may also contribute to the capping structure to prevent amyloid-like polymerization.
 


Within the core there are <scene name='60/607864/Hydrogen_bonds/1'>hydrogen bonds</scene> between Thr-Ser (65-55, 85-75, 132-124 respectively) and one <scene name='60/607864/Disulfide_bond/1'>disulfide bond</scene> between Cys4-Cys21, that contributes to stabilize the whole structure.   
Within the core there are <scene name='60/607864/Hydrogen_bonds/1'>hydrogen bonds</scene> between Thr-Ser (65-55, 85-75, 132-124 respectively) and one <scene name='60/607864/Disulfide_bond/1'>disulfide bond</scene> between Cys4-Cys21, that contributes to stabilize the whole structure.