User:Rana Saad/The human GABAb receptor

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This is a default text for your page '''Human gabab receptor'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs.
This is a default text for your page '''Human gabab receptor'''. 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 <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
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==Introduction==
==Introduction==
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γ-Aminobutyric acid (GABA)
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===γ-Aminobutyric acid (GABA)===
GABA is the major inhibitory neurotransmitter in the central nervous system (CNS). It plays a key role in modulating neuronal activity since it binds to specific transmembrane receptors (GABAa,,GABAb and GABAc) in the plasma membrane of both pre- and postsynaptic neuronal level.
GABA is the major inhibitory neurotransmitter in the central nervous system (CNS). It plays a key role in modulating neuronal activity since it binds to specific transmembrane receptors (GABAa,,GABAb and GABAc) in the plasma membrane of both pre- and postsynaptic neuronal level.
• GABAb receptors
• GABAb receptors
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== Function ==
== Function ==
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GABAb functions as an obligatory heterodimer subunit of GBR1, which is responsible for ligand-binding. GBR2, on the other hand, is responsible for G protein coupling subunits. (see pictures 1)
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GABAb functions as an obligatory heterodimer subunit of GBR1, which is responsible for ligand-binding. GBR2, on the other hand, is responsible for G protein coupling subunits.
GBR1 and GBR2 subunits structure: Each subunit is a domain of seven-transmembrane helixes, composed of a large extracellular domain - venus flytrap (VFT)
GBR1 and GBR2 subunits structure: Each subunit is a domain of seven-transmembrane helixes, composed of a large extracellular domain - venus flytrap (VFT)

Revision as of 11:33, 5 May 2015

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Caption for this structure

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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

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Rana Saad

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