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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
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Drugs Affecting Neurotransmitter Synthesis

Drugs affecting neurotransmitter synthesis can impact the adrenergic neuron and the synthesis of neurotransmitters. For example, α-methyltyrosine and carbidopa target specific enzymes involved in catecholamine synthesis. α-methyltyrosine inhibits the enzyme tyrosine hydroxylase, which converts tyrosine into dopamine. By blocking this enzyme, α-methyltyrosine reduces dopamine production and other catecholamines. Carbidopa, on the other hand, inhibits the enzyme dopa decarboxylase, which converts...
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
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Interaction domains in cell signaling
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Related Experiment Video

Updated: Jun 8, 2026

Identification of Dopamine D1-Alpha Receptor Within Rodent Nucleus Accumbens by an Innovative RNA In Situ Detection Technology
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The dopamine D(4) receptor, the ultimate disordered protein.

Amina S Woods1

  • 1Structural Biology Unit, Cellular Neurobiology Branch, NIDA IRP, NIH, Baltimore, MD 21224, USA. awoods@intra.nida.nih.gov

Journal of Receptor and Signal Transduction Research
|September 15, 2010
PubMed
Summary

The human D4 dopamine receptor (D4R) has unique gene variants in its third intracellular loop (IL3). This proline-rich region

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Genetics

Background:

  • The D4 dopamine receptor (D4R) is crucial for neuronal signaling in the brain's mesolimbic system, regulating emotion and behavior.
  • D4R is a G protein-coupled receptor (GPCR) with unique polymorphic variants in its third intracellular loop (IL3).
  • The IL3 region of D4R is unusually proline-rich and contains multiple 48 base pair repeats, contributing to a high disorder index.

Purpose of the Study:

  • To investigate the structural and functional significance of the polymorphic variants in the D4 dopamine receptor's third intracellular loop (IL3).
  • To explore the unique proline-rich nature of the D4R IL3 and its implications for protein-protein interactions.
  • To understand the role of the D4R IL3 region in receptor interactions, drawing parallels with the D2 receptor (D2R).

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Generation, Purification, and Characterization of Cell-invasive DISC1 Protein Species
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Published on: August 30, 2012

Main Methods:

  • Bioinformatic analysis of D4R gene sequences to identify and characterize polymorphic variants in the IL3 region.
  • Protein structure prediction and disorder analysis to assess the impact of repeats on IL3 structure.
  • Comparative analysis of IL3 sequences and properties across different GPCRs, including D2R.

Main Results:

  • The D4 receptor (D4R) exhibits significant genetic polymorphism in its third intracellular loop (IL3), characterized by variable numbers of 48 base pair repeats.
  • These repeats result in a highly disordered and proline-rich IL3 region, a unique feature among GPCRs.
  • The high disorder index suggests increased potential for interactions with other proteins.

Conclusions:

  • The polymorphic and proline-rich IL3 region of the D4 dopamine receptor (D4R) is a key determinant of its unique structural and interactive properties.
  • This region's characteristics likely play a significant role in D4R's function within the mesolimbic system.
  • Further research into D4R IL3 interactions may reveal novel insights into neurotransmitter receptor signaling and function.