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{{Template:CH462_Biochemistry_II_2023}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE -->
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{{BAMBED
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==Your Heading Here (maybe something like 'Structure')==
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|DATE=June 14, 2016
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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|OLDID=2607465
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This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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|BAMBEDDOI=10.1002/bmb.21026
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You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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}}
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== Function ==
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==SHOC2-PP1C-MRAS==
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== Disease ==
 
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== Relevance ==
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== Introduction ==
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'''Receptor Tyrosine Kinase Receptor'''
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*[[Lipid signaling]]
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*[[Transmembrane (cell surface) receptors]]
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== Structural highlights ==
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[[Image:LPA_in_membrane4.fw.png|200px|center|thumb|'''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.]]
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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.
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== Lysophosphatidic Acid ==
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[[Image:LPA.png|220px|left|thumb|'''Figure 2:''' Chemical Structure of LPA (monoacyl-sn-glycero-3-phosphate)]]
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== Overall Structure ==
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=== SHOC2 ===
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=== PP1C ===
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=== MRAS ===
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=== Key Ligand Interactions ===
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[[Image:Amphbindingfinal.png|275 px|right|thumb|'''Figure 3''': Electrostatic illustration of the amphipathic binding pocket of the LPA<sub>1</sub> 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.]]
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=== SHOC2 and PP1C ===
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=== SHOC2 and MRAS ===
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=== PP1C and MRAS ===
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== Signaling Pathway ==
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== Disease Relevance ==
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=== Cancer ===
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=== RASopathies===
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== Future Studies ==
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==3D structures of lysophosphatidic acid receptor==
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[[4z34]], [[4z35]], [[4z36]] - hLPA1 + antagonist - human<br />
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[[2lq4]] – hLPA1 second extracellular loop – NMR<br />
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[[4p0c]] – hLPA2/NHERF2<br />
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[[5xsz]] – LPA6A (mutant) – zebra fish<br />
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</StructureSection>
 
== References ==
== References ==
<references/>
<references/>
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==Proteopedia Resources==
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[http://proteopedia.org/wiki/index.php/Category:Lysophosphatidic_acid_binding Category:Lysophosphatidic acid binding]
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[http://proteopedia.org/wiki/index.php/Category:Lysophosphatidic_acid Category:Lysophosphatidic acid]
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[http://proteopedia.org/wiki/index.php/User:R._Jeremy_Johnson/CH462:Biochemistry_II_Butler_University Butler University Proteopedia Pages]
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See also:
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*[[Receptor]]
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*[[Transmembrane (cell surface) receptors]]
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*[[G protein-coupled receptors]]
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</StructureSection>
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==Student Contributors==
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Madeline Gilbert
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Inaya Patel
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Rushda Hussein
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[[Category:Featured in BAMBED]]
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[[Category:Topic Page]]

Revision as of 16:56, 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

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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