Human dopamine D2 receptor (D₂R) gene has polymorphic variants, three of them alter its amino acid sequence: Val96Ala, Pro310Ser and Ser311Cys. Their functional role never became the object of extensive studies, even though there are some evidence that they correlate with schizophrenia. The present work reviews data indicating that these mutations play a role in dimer formation with dopamine D1 receptor (D₁R), with the strongest effect observed for Ser311Cys variant. Similarly, the affinity for antipsychotic drugs of this genetic variant depends on whether it is expressed together with D₁R or not. Better understanding of altered ability of genetic variants of D₂R to form dimers with D₁R, as well as of altered affinity for antipsychotic drugs, depending on the absence or presence of the second dopamine receptor is of great importance—since these two receptors are not always co-expressed in the same cell. It may well be that targeting new compounds toward the D₁R-D₂R dimers, which the most probably form under conditions of excessive dopamine release, will result in antipsychotic drugs devoid of serious side effects.

人多巴胺D2受体（D ₂ R）基因具有多态性变体，其中三个改变其氨基酸序列：Val96Ala，Pro310Ser和Ser311Cys。尽管有一些证据表明它们与精神分裂症有关，但它们的功能作用从未成为广泛研究的对象。本工作回顾了表明这些突变在与多巴胺D1受体（D ₁ R）形成二聚体中起作用的数据，其中Ser311Cys变体的作用最强。类似地，该遗传变异体对抗精神病药的亲和力取决于它是否与D ₁ R一起表达。更好地了解D ₂ R的遗传变异与D ₁形成二聚体的能力改变R以及对抗精神病药物的亲和力改变取决于第二多巴胺受体的存在与否，这一点非常重要-因为这两种受体并非总是在同一细胞中共表达。很有可能将新化合物靶向D ₁ R-D ₂ R二聚体（最可能在多巴胺过量释放的条件下形成），将导致抗精神病药缺乏严重副作用。