Sandbox 5

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[[Image:1ema BIOmics 5.gif|350px]]
 
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HER2 is a member of epidermal growth factor receptor
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Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
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<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='Sandbox_5/Green_fluorescent_protein/2'>chromophore</scene>, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues.<ref>PMID:8703075</ref>
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<ref>PMID:8703075</ref>
== References ==
== References ==
<references/>
<references/>
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<scene name='10/101618/Scene1/3'>Herceptin Fab binds HER2</scene>
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<scene name='10/101618/Scene1/4'>The Herceptin-binding site.</scene>Herceptin binds to juxtamembrane region of HER2

Revision as of 08:35, 23 May 2014

HER2 is a member of epidermal growth factor receptor


Exploring the Structure

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Drag the structure with the mouse to rotate

[1]

References

  1. ↑ Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075

Herceptin binds to juxtamembrane region of HER2

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