User:Caitlin Marie Gaich/Sandbox1

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== Introduction ==
== Introduction ==
[https://en.wikipedia.org/wiki/Histone Histone background]
[https://en.wikipedia.org/wiki/Histone Histone background]
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== Function ==
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== HAT1 Background ==
[[Image:Main_bonding_cartoon_3.png|400px|right|thumb|Figure 1]]
[[Image:Main_bonding_cartoon_3.png|400px|right|thumb|Figure 1]]
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== Disease ==
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== Hat1/Hat2 Complex Structure ==
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== Relevance ==
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== Structural highlights ==
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Histone acetyltransferase has an elongated, curved structure with the N and C termini on opposite ends of the structure.
Histone acetyltransferase has an elongated, curved structure with the N and C termini on opposite ends of the structure.
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.
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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</StructureSection>
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</Hat1/Hat2 Complex StructureSection>
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== Mechanism ==
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== Application ==
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== References ==
== References ==
Li, Y. et. al. ''Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.''(2014). ''Genes Dev.''28:1217-1227. DOI:10.1101/gad.240531.114
Li, Y. et. al. ''Hat2p recognizes the histone H3 tail to specify the acetylation of the newly synthesized H3/H4 heterodimer by the Hat1p/Hat2p complex.''(2014). ''Genes Dev.''28:1217-1227. DOI:10.1101/gad.240531.114

Revision as of 17:40, 29 March 2019

Histone Acetyltransferase HAT1/HAT2 Complex, Saccharomyces cerevisiae

HAT1 4PSW

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Caitlin Marie Gaich

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