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== Signaling Pathway ==
== Signaling Pathway ==
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[[Image:Dephosphorylation.png|380 px|thumb|center|'''Figure 1:'''Comparison of Delta-opioid receptor to human free-fatty acid receptor (hGPR40) both of which are G-protein coupled receptors. The binding pocket of the delta-opioid receptor is solvent exposed allowing ligands to enter directly from the extracellular space while the binding pocket of hGPR40 is covered by the extracellular loop 2 (ECL2) preventing entry from the extracellular space (ECL2 represented in cyan). The Delta-opioid displays the canonical binding site typical of most GPCRs while ligands of hGPR40 bind to a noncanonical pocket represented in pink.]]

Revision as of 17:06, 17 March 2023

This page, as it appeared on June 14, 2016, was featured in this article in the journal Biochemistry and Molecular Biology Education.

Contents

SHOC2-PP1C-MRAS

Introduction

Receptor Tyrosine Kinase Receptor

Figure 1: LPA receptor (blue) bound to the cell membrane. The binding pocket is highlighted in red. The added bRIL protein is highlighted in orange.
Figure 1: LPA receptor (blue) bound to the cell membrane. The binding pocket is highlighted in red. The added bRIL protein is highlighted in orange.

Lysophosphatidic Acid

Figure 2: Chemical Structure of LPA (monoacyl-sn-glycero-3-phosphate)
Figure 2: Chemical Structure of LPA (monoacyl-sn-glycero-3-phosphate)


Overall Structure

SHOC2

PP1C

MRAS

Key Ligand Interactions

Figure 3: Electrostatic illustration of the amphipathic binding pocket of the LPA1 receptor. This binding pocket was revealed by cutting away the exterior or the protein. This binding pocket, located in the interior of the protein, has both polar and nonpolar regions. The blue and red coloration highlight the positively and negatively charged regions, respectively, and the white color shows the nonpolar region of the binding pocket.
Figure 3: Electrostatic illustration of the amphipathic binding pocket of the LPA1 receptor. This binding pocket was revealed by cutting away the exterior or the protein. This binding pocket, located in the interior of the protein, has both polar and nonpolar regions. The blue and red coloration highlight the positively and negatively charged regions, respectively, and the white color shows the nonpolar region of the binding pocket.

SHOC2 and PP1C

SHOC2 and MRAS

PP1C and MRAS

Signaling Pathway

Figure 1:Comparison of Delta-opioid receptor to human free-fatty acid receptor (hGPR40) both of which are G-protein coupled receptors. The binding pocket of the delta-opioid receptor is solvent exposed allowing ligands to enter directly from the extracellular space while the binding pocket of hGPR40 is covered by the extracellular loop 2 (ECL2) preventing entry from the extracellular space (ECL2 represented in cyan). The Delta-opioid displays the canonical binding site typical of most GPCRs while ligands of hGPR40 bind to a noncanonical pocket represented in pink.
Figure 1:Comparison of Delta-opioid receptor to human free-fatty acid receptor (hGPR40) both of which are G-protein coupled receptors. The binding pocket of the delta-opioid receptor is solvent exposed allowing ligands to enter directly from the extracellular space while the binding pocket of hGPR40 is covered by the extracellular loop 2 (ECL2) preventing entry from the extracellular space (ECL2 represented in cyan). The Delta-opioid displays the canonical binding site typical of most GPCRs while ligands of hGPR40 bind to a noncanonical pocket represented in pink.



Disease Relevance

Cancer

RASopathies

Future Studies

3D structures of lysophosphatidic acid receptor

4z34, 4z35, 4z36 - hLPA1 + antagonist - human
2lq4 – hLPA1 second extracellular loop – NMR
4p0c – hLPA2/NHERF2
5xsz – LPA6A (mutant) – zebra fish

References

Proteopedia Resources

Category:Lysophosphatidic acid binding

Category:Lysophosphatidic acid

Butler University Proteopedia Pages

See also:

</StructureSection>

Student Contributors

Madeline Gilbert Inaya Patel Rushda Hussein

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