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A cluster of aromatic residues in the sixth membrane-spanning segment of the dopamine D2 receptor is accessible in the binding-site crevice.

Abstract：

:The binding site of the dopamine D2 receptor, like that of other homologous G protein-coupled receptors, is contained within a water-accessible crevice formed among its seven membrane-spanning segments. Using the substituted-cysteine accessibility method, we previously mapped the residues in the third, fifth, and seventh membrane-spanning segments that contribute to the surface of this binding-site crevice. We have now mutated to cysteine, one at a time, 22 consecutive residues in the sixth membrane-spanning segment (M6) and expressed the mutant receptors in HEK 293 cells. Ten of these mutants reacted with charged, hydrophilic, lipophobic, sulfhydryl-specific reagents, added extracellularly, and all but one were protected from reaction by a reversible dopamine antagonist, sulpiride. Thus, we infer that the side chains of the residues at the reactive loci (V378, F382, W386, P388, F389, F390, T392, H393, I394, and I397) are on the water-accessible surface of the binding-site crevice. The pattern of accessibility is consistent with an alpha-helical conformation with a wide angle of accessibility near the binding site itself and a narrower stripe continuing toward the cytoplasmic portion of the binding-site crevice. This pattern of accessibility is consistent with the presence of a proline kink which could bend the extracellular portion of M6 into the binding-site crevice where it would be more broadly accessible than the cytoplasmic portion of the membrane-spanning segment. Four highly conserved aromatic residues and a histidine are clustered together on the water-accessible surface of the binding-site crevice. They define an interconnected "aromatic cluster" that may be involved in ligand binding and receptor activation.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Javitch JA,Ballesteros JA,Weinstein H,Chen J

doi

10.1021/bi972241y

subject

Has Abstract

pub_date

1998-01-27 00:00:00

pages

998-1006

issue

4

eissn

0006-2960

issn

1520-4995

pii

bi972241y

journal_volume

37

pub_type

杂志文章

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