Sandbox Reserved 474: Difference between revisions
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== Structure of CRP pentamer == | == Structure of CRP pentamer == | ||
In CRP, each subunit in CRP is rotated by 22° towards the five-fold axis in comparison to SAP, where the subunits are planar to each other [1]. Furthermore, an intermoleclar ion pair only forms in CRP from residues <scene name='Sandbox_Reserved_474/Glu-197/1'>Glu-197</scene> and <scene name='Sandbox_Reserved_474/Lys-123/1'>Lys-123</scene>, but this does not occur in SAP. One could deduce that by crystallizing the structure, it causes a shift of the actual ligand-binding sites on the B side of the pentamer which can effect overall binding to other significant structures. | In CRP, each subunit in CRP is rotated by 22° towards the five-fold axis in comparison to SAP, where the subunits are planar to each other [1]. Furthermore, an intermoleclar ion pair only forms in CRP from residues <scene name='Sandbox_Reserved_474/Glu-197/1'>Glu-197</scene> and <scene name='Sandbox_Reserved_474/Lys-123/1'>Lys-123</scene>, but this does not occur in SAP. One could deduce that by crystallizing the structure, it causes a shift of the actual ligand-binding sites on the B side of the pentamer which can effect overall binding to other significant structures. | ||
== Phosphocholine-binding == | |||
It is worthy to note that the major interaction that occurs between CRP and PC is located between the phosphate group of PC and the bound calciums [1]. While the majority of the PC molecule is packed tightly against Phe-66, the rest of the molecule binds thus resulting in a phosphate moiety ester linkage [1]. The overall distance between the the charged nitrogen of PC and the acidic Glu-81 is approximately 3.8 Å and this suggests that this particular interaction is important. Because of this physical phenomenon, future drugs could be developed to potentially block the CRP from binding. | |||
== Comparison of human CRP to other pentraxins == | == Comparison of human CRP to other pentraxins == | ||
