User:Anat Levit/Sandbox 1: Difference between revisions

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The prokineticin and their receptors are expressed in various tissues, including the cardiovascular, gastrointestinal, immune, reproductive, endocrine and nervous systems. The receptors have been shown to couple to Gq, Gi and Gs, thereafter mediating intracellular calcium mobilization, phosphorylation of p42/p44 MAPK, AKT and cAMP accumulation, respectively. Receptor activation has been shown to mediate proliferation, anti-apoptosis, differentiation and mobilization of target cells.

The prokineticin receptors have been found to be involved in various pathologies involving the cardiovascular, reproductive, endocrine and nervous systems. Notably, PROKR2 has been found to be <scene name='User:Anat_Levit/Sandbox_1/~~Pkr_ks_mutations~~/4'>mutated in Kallmann syndrome</scene> with dilated cardiomyopathy, a hypogonadism caused by a deficiency of gonadotropin-releasing hormone (GnRH) (see Wikipedia:

The prokineticin receptors have been found to be involved in various pathologies involving the cardiovascular, reproductive, endocrine and nervous systems. Notably, PROKR2 has been found to be <scene name='User:Anat_Levit/Sandbox_1/Pkr1_ks_mutations/1'>mutated in Kallmann syndrome</scene> with dilated cardiomyopathy, a hypogonadism caused by a deficiency of gonadotropin-releasing hormone (GnRH) (see Wikipedia:

[http://en.wikipedia.org/wiki/Kallmann_syndrome Kallmann syndrome]). Except for V331M and R357W which are Leu and Asn in PROKR1, respectively, all other residues mutated in PROKR2 are identical in PROKR1. Interestingly, two of the mutated residues, W178 (4.50) and P290 (6.50), are two of the most conserved residues in family A GPCRs (<scene name='User:Anat_Levit/Sandbox_1/Pkr_colored_by_homology/4'>restore initial scene</scene>).

[[Image:ColorKey_ConSurf_NoYellow_NoGray.gif|right|200 px]]

Being highly homologues proteins, expressed in the same cell types and having similar nano-molar affinity to common ligands, it is of importance to understand the structural and functional differences between these receptors.

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 The prokineticin and their receptors are expressed in various tissues, including the cardiovascular, gastrointestinal, immune, reproductive, endocrine and nervous systems. The receptors have been shown to couple to Gq, Gi and Gs, thereafter mediating intracellular calcium mobilization, phosphorylation of p42/p44 MAPK, AKT and cAMP accumulation, respectively. Receptor activation has been shown to mediate proliferation, anti-apoptosis, differentiation and mobilization of target cells.
-The prokineticin receptors have been found to be involved in various pathologies involving the cardiovascular, reproductive, endocrine and nervous systems. Notably, PROKR2 has been found to be <scene name='User:Anat_Levit/Sandbox_1/Pkr_ks_mutations/4'>mutated in Kallmann syndrome</scene> with dilated cardiomyopathy, a hypogonadism caused by a deficiency of gonadotropin-releasing hormone (GnRH) (see Wikipedia:
+The prokineticin receptors have been found to be involved in various pathologies involving the cardiovascular, reproductive, endocrine and nervous systems. Notably, PROKR2 has been found to be <scene name='User:Anat_Levit/Sandbox_1/Pkr1_ks_mutations/1'>mutated in Kallmann syndrome</scene> with dilated cardiomyopathy, a hypogonadism caused by a deficiency of gonadotropin-releasing hormone (GnRH) (see Wikipedia:
 [http://en.wikipedia.org/wiki/Kallmann_syndrome Kallmann syndrome]). Except for V331M and R357W which are Leu and Asn in PROKR1, respectively, all other residues mutated in PROKR2 are identical in PROKR1. Interestingly, two of the mutated residues, W178 (4.50) and P290 (6.50), are two of the most conserved residues in family A GPCRs (<scene name='User:Anat_Levit/Sandbox_1/Pkr_colored_by_homology/4'>restore initial scene</scene>).
 [[Image:ColorKey_ConSurf_NoYellow_NoGray.gif|right|200 px]]
 Being highly homologues proteins, expressed in the same cell types and having similar nano-molar affinity to common ligands, it is of importance to understand the structural and functional differences between these receptors.