User:Allison Welz/Sandbox 1
From Proteopedia
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=== Mutations === | === Mutations === | ||
| - | == | + | ====D201V==== |
| - | + | <scene name='87/877636/D201_mutation/10'>D201V</scene> is a mutation that is found to cause [https://en.wikipedia.org/wiki/Lipoprotein_lipase_deficiency chylomicronemia]. Chylomicronemia is when the body cannot break down lipids properly. This leads to their build-up in the body causing high levels of triglycerides in the body. The [https://en.wikipedia.org/wiki/Aspartic_acid carboxyl side chain of aspartate] 201 is one of the coordination sites for the calcium ion of LPL. The mutation to hydrophobic [https://en.wikipedia.org/wiki/Valine valine] means the loss of this coordination site<ref name="Birrane">PMID:30559189</ref>. This mutation adversely affects the folding of LPL and thus affects the secretion of LPL, overall decreasing the activity of LPL<ref name="Birrane">PMID:30559189</ref>. | |
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| + | ====M404R==== | ||
| + | <scene name='87/877636/M404r_1/2'>M404R</scene> is a mutation found within LPL that caused [https://en.wikipedia.org/wiki/Lipoprotein_lipase_deficiency chylomicronemia] in patients. The hydrophobic [https://en.wikipedia.org/wiki/Methionine methionine] is mutated to the larger and charged side chain of [https://en.wikipedia.org/wiki/Arginine arginine]. Originally it was thought to impact LPL secretion from cells. It was found that the M404R does not affect LPL secretion <ref name="Birrane">PMID:30559189</ref>. M404R interacts with the hydrophobic pocket of GPIHBP1’s finger 3 of its 3 fingered domain (V121, E122, T124, V126). The large, charged arginine repelled the hydrophobic pocket and does not fit well. This prevents proper binding and formation of the LPL-GPIHBP1 complex <ref name="Birrane">PMID:30559189</ref>. | ||
</StructureSection> | </StructureSection> | ||
Revision as of 21:18, 26 April 2021
Contents |
LPL with GPIHBP-1, Drosophilia S2
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M404R Mutation
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Relevance
Structural highlights
</StructureSection>
Student Contributors
- Ashrey Burley
- Allison Welz
- Hannah Wright
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.
</StructureSection>
References
- ↑ 1.0 1.1 1.2 1.3 Birrane G, Beigneux AP, Dwyer B, Strack-Logue B, Kristensen KK, Francone OL, Fong LG, Mertens HDT, Pan CQ, Ploug M, Young SG, Meiyappan M. Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis. Proc Natl Acad Sci U S A. 2018 Dec 17. pii: 1817984116. doi:, 10.1073/pnas.1817984116. PMID:30559189 doi:http://dx.doi.org/10.1073/pnas.1817984116
