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From Proteopedia

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'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.

Structure of Steroid Receptor Hormone

This is a default text for your page '. Click above on edit this page' to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia ^[1] or to the article describing Jmol ^[2] to the rescue.

Function

Steroid Hormone receptors overlook and control gene expression, the rate of cellular reproduction, and specialization in eukaryotes. The receptors do so by turning genes controlled by particular promoters on or off as steroid molecules (hormones) bind to them. Steroid hormone receptors therefore serve as transcription factors containing zinc fingers which are repeated structural units.

The estrogen receptor (ER) is found in the heat shock protein complex found in the nucleus. When the ligand binds to the ER, it undergoes a conformational change which displaces the heat shock protein complex allowing cofactors to bind and facilitate the receptors interaction with desired genes. When the oestrogen ligand is present, the oestrogen receptor regulates gene expression by either recognizing and binding to the DNA palindromic estrogen response element sequence (ERE) or by interacting with other transcription factors.

In terms of ligand-independent activity, the ER uses many different intracellular signalling pathways which use either the phosphorylation of the ER by protein kinases or regulation of the ER-bound cofactors to produce various cell and tissue specific oestrogenic responses. For example, the activation of the epidermal growth factor (EGF) receptor leads to ER𝛂 phosphorylation through the mitogen-activated protein kinase (MAPK) pathway which enhances the ER interaction with the steroid receptor co activator, thereby affecting ligand binding. Feedback also occurs where oestrogen activates MAPK pathway which activates the ER and amplifies the pathway signal.

Interactions

Steroid hormone receptors regulate gene transcription through various interaction including binding to the hormone, binding to itself to form a homodimer, binding to its response element, or binding to other protein cofactors. Examples of ligand molecules for steroid hormone receptors include aldosterone, estrogen, the thyroid hormone T3, calcitriol, the active form of vitamin D, and retinol.

Interaction Location

The receptors perform their interactions within the nucleus independent of the heat shock protein complex in order to control gene expression.

Origin

48 steroid hormone and nuclear receptor genes have been revealed in humans. The highly conserved DNA binding domains and the ligand binding domains indicate that the steroid hormone receptors share a common ancestral molecule.

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References

1. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
2. ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644