User:Justin Smith/Sandbox 1

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Contents 1 DGAT Homo Sapien 2 Disease 3 Active Site 4 Relevance 5 Mecanism 6 Structural highlights 7 References 8 Student Contributers

DGAT Homo Sapien

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function The triacylglycerol biosynthesis pathway was elucidated nearly 60 years ago Excessive Triglycerides = Obesity and Metabolic diseases DGAT enzymes were identified more than 20 years ago Polytopic Endoplasmic Reticulum Membrane Protein Embedded in membrane of ER Highly Expressed in Epithelial cells, small intestine, and liver, female mammary glands

Disease

Active Site

is the active base catalytic function

Relevance

Mecanism

Structural highlights

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References

Wang, L, Qian, H, Nian, Y, Han, Y, Ren, Z, Hanzhi, Z, Hu, L, Prasad, B.V., Laganowsky, A, Yan, N, Zhou, M. (2020). Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature, 581, 329-332. ^[1].

Sui, X, Wang, K, Gluchowski, N, Elliott, S, Liao, M, Walther, T, Farese Jr, R. (2020). Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature, 581, 323-328.

Rodriguez, A. M. (2020). Zooming in on the architecture of DGAT1, a transmembrane lipid factory. Baylor College of Medicine.

Stone, S. J. Mammalian Diacylglycerol Acyltransferases (DGAT). AOCS Lipid Library.

1. ↑ Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, Hu L, Prasad BVV, Laganowsky A, Yan N, Zhou M. Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature. 2020 May;581(7808):329-332. doi: 10.1038/s41586-020-2280-2. Epub 2020 May, 13. PMID:32433610 doi:http://dx.doi.org/10.1038/s41586-020-2280-2

Student Contributers

• Justin Smith