Sandbox Reserved 1290

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==Human core-PIC in the initial transcribing state (no IIS)==
==Human core-PIC in the initial transcribing state (no IIS)==
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<scene name='75/751183/P_chain/2'>P Chain</scene>
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<scene name='75/751183/M_chain/1'>M Chain</scene>
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<Structure load='5iyd='350' frame='true' align='right' caption='Pictured above is a thing' scene='Hey here's a thing' />{{Sandbox_Reserved_O'Brochta_HLSC322}}
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<Structure load='5iyd='350' frame='true' align='right' caption='Pictured above is a thing' scene='Hey here's a thing' />{{Sandbox_Reserved_O'Brochta_HLSC322}}
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<scene name='75/751183/M_chain/1'>TextToBeDisplayed</scene>
== Function ==
== Function ==

Revision as of 22:13, 9 February 2017

Contents

Human core-PIC in the initial transcribing state (no IIS)

Pictured above is a thing

Drag the structure with the mouse to rotate
==genetics is ok==

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION


'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.


'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.


Specific are highlighted here. The ligands listed above, GDP, Phe, and Mg+2 ion each attach at these locations which are still being explored.

which play a crucial role in binding to the ribosome during translation. They form positive pockets with which negative amino acids can bind to.

'Molecules it Interacts With and where '

The protein binds to GDP as well as the following ligands in order to promote the attachment of the protein complex to the ribosome A site.

PHOSHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


PHENYLALANINE MAGNESIUM ION


'Origin'

It has domains that are created in yeast (phenyl-transfer RNA) , in the heat resistant Thermus aquaticus (EF-Tu elongation factor, and can be synthetically manufactured.


'Structure'

It has 3 domains. G proteins, Elongation Factors, and the EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain. It is composed of 6 chains, which combine in alignment.


Specific are highlighted here.

which play a crucial role in binding to the ribosome during translation.

'Function"

The protein complex participates in placing the amino acids in their correct order when messenger RNA is translated into a protein sequence on the ribosome by promoting GTP-dependent binding of tRNA to the A site of the ribosome. In other words, it is involved with elongation during polypeptide synthesis.

Phe-tRNA, elongation factor EF-TU:GDPNP Ternary complex

Drag the structure with the mouse to rotate

Function

Human core-PIC helps in the transcription of DNA into using four ribonucleotide triphosphates as substrates. The molecule is a component of RNA Polymerase II, and thus is integral in the synthesis of mRNA precursors and functional non-coding RNA.

What it Interacts With

Human core-PIC interacts with DNA, ribonucleotide triphosphates, mRNA, and DNA Polymerase II

Where is interacts

The molecule interacts with DNA in the nucleus, where the mRNA transcript is synthesized.

Where it originates

Human core-PIC originates in homo sapiensis, or the modern day human.

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

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