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9.A.14.3.9
The dopamine receptor D3, DRD3 or D3R of 400 aas.  Residues involved in receptor signaling have been identified (Kota et al. 2015), and several agonists are known (Xu et al. 2016). The atomic-level dopamine activation mechanism for transmitting extracellular ligand binding events through transmembrane helices to the cytoplasmic G protein has been elucidated (Weng et al. 2017). In agonist-bound systems, the D3R N-terminus forms a "lid-like" structure and lies flat on the binding site opening, whereas in antagonist-bound systems, the N-terminus exposes the binding cavity. A continuous water pathway is present only in the dopamine-Galphai-bound system. In the inactive D3Rs, water entry is hindered by the hydrophobic layers. It was proposed that upon agonist binding, the "lid-like" conformation of the N-terminus induces a series of molecular switches to increase the volume of the D3R cytoplasmic binding part for G protein association. Water enters the transmembrane region, inducing molecular switches to assist in opening the hydrophobic layers to form a continuous water channel, which is crucial for maintaining a fully active conformation for signal transduction (Weng et al. 2017). S-Deoxyephedrine can move through molecular channels within D3R (Li et al. 2017).

Accession Number:P35462
Protein Name:D(3) dopamine receptor
Length:400
Molecular Weight:44225.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate NONE

Cross database links:

Structure:
3PBL     

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MASLSQLSSH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL 
61:	QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN 
121:	LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV 
181:	CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ 
241:	QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK 
301:	LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV 
361:	SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC