Sandbox Reserved 474: Difference between revisions

Line 10:

== Structure and Function ==

CRPs five promoter structures are folded into two anti-parallel <scene name='Sandbox_Reserved_474/Beta-sheet/1'>β-Sheets</scene> with flattened jellyroll topologies [2]. Each promoter contains a recognition face with a <scene name='Sandbox_Reserved_474/Phosphocholine/1'>phosphocholine</scene> binding site consisting of two coordinated <scene name='Sandbox_Reserved_474/Calcium_ion/1'>calcium </scene> ions adjacent to a hydrophobic pocket.

The co-crystallized structure of CRP with phosphocholine suggest that <scene name='Sandbox_Reserved_474/Phe-66/2'>Phe-66</scene> and <scene name='Sandbox_Reserved_474/Glu-81/1'>Glu-81</scene> are two very crucial residues that mediate binding between phosphocholine and CRP[2]. More specifically, Phe-66 provides specific hydrophobic interactions with the methyl groups of PC. Similarly, Glu-81 is located on the opposite end of the pocket where it interacts well with the positively charged choline nitrogen. Present on the opposite face of the pentamer is the effector face, where the presumed <scene name='Sandbox_Reserved_474/C1q/1'>C1q</scene> and Fcγ receptors bind, and at this cleft ~~are~~ several residues present (<scene name='Sandbox_Reserved_474/Asp-112/1'>Asp-112</scene> and Tyr-175) which are both necessary to bind CRP to C1q [2].

The co-crystallized structure of CRP with phosphocholine suggest that <scene name='Sandbox_Reserved_474/Phe-66/2'>Phe-66</scene> and <scene name='Sandbox_Reserved_474/Glu-81/1'>Glu-81</scene> are two very crucial residues that mediate binding between phosphocholine and CRP[2]. More specifically, Phe-66 provides specific hydrophobic interactions with the methyl groups of PC. Similarly, Glu-81 is located on the opposite end of the pocket where it interacts well with the positively charged choline nitrogen. Present on the opposite face of the pentamer is the effector face, where the presumed <scene name='Sandbox_Reserved_474/C1q/1'>C1q</scene> and Fcγ receptors bind, and at this cleft several residues are present (<scene name='Sandbox_Reserved_474/Asp-112/1'>Asp-112</scene> and Tyr-175) which are both necessary to bind CRP to C1q [2].

== Mechanism ==

Sandbox Reserved 474: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 10: / Line 10: @@
 == Structure and Function ==
 CRPs five promoter structures are folded into two anti-parallel <scene name='Sandbox_Reserved_474/Beta-sheet/1'>β-Sheets</scene> with flattened jellyroll topologies [2].  Each promoter contains a recognition face with a <scene name='Sandbox_Reserved_474/Phosphocholine/1'>phosphocholine</scene> binding site consisting of two coordinated <scene name='Sandbox_Reserved_474/Calcium_ion/1'>calcium </scene> ions adjacent to a hydrophobic pocket.
-The co-crystallized structure of CRP with phosphocholine suggest that <scene name='Sandbox_Reserved_474/Phe-66/2'>Phe-66</scene> and <scene name='Sandbox_Reserved_474/Glu-81/1'>Glu-81</scene> are two very crucial residues that mediate binding between phosphocholine and CRP[2].  More specifically, Phe-66 provides specific hydrophobic interactions with the methyl groups of PC.  Similarly, Glu-81 is located on the opposite end of the pocket where it interacts well with the positively charged choline nitrogen.  Present on the opposite face of the pentamer is the effector face, where the presumed <scene name='Sandbox_Reserved_474/C1q/1'>C1q</scene> and Fcγ receptors bind, and at this cleft are several residues present (<scene name='Sandbox_Reserved_474/Asp-112/1'>Asp-112</scene> and Tyr-175) which are both necessary to bind CRP to C1q [2].
+The co-crystallized structure of CRP with phosphocholine suggest that <scene name='Sandbox_Reserved_474/Phe-66/2'>Phe-66</scene> and <scene name='Sandbox_Reserved_474/Glu-81/1'>Glu-81</scene> are two very crucial residues that mediate binding between phosphocholine and CRP[2].  More specifically, Phe-66 provides specific hydrophobic interactions with the methyl groups of PC.  Similarly, Glu-81 is located on the opposite end of the pocket where it interacts well with the positively charged choline nitrogen.  Present on the opposite face of the pentamer is the effector face, where the presumed <scene name='Sandbox_Reserved_474/C1q/1'>C1q</scene> and Fcγ receptors bind, and at this cleft several residues are present (<scene name='Sandbox_Reserved_474/Asp-112/1'>Asp-112</scene> and Tyr-175) which are both necessary to bind CRP to C1q [2].
 == Mechanism ==