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TitleTransport and inhibition mechanisms of human glycine transporter 2.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateApr 16, 2026
AuthorsWenming Ji / Yuanzhi Yu / Zirui Liu / Junwen Su / Qianyu Wang / Mulin Lai / Jing-Xiang Wu /
PubMed AbstractNeuronal human glycine transporter 2 (hGlyT2) plays a critical role in maintaining glycinergic neurotransmission via the reuptake of glycine into presynaptic neurons by using the driving force of ...Neuronal human glycine transporter 2 (hGlyT2) plays a critical role in maintaining glycinergic neurotransmission via the reuptake of glycine into presynaptic neurons by using the driving force of sodium and chloride ion gradients. hGlyT2 represents an important drug target for analgesic purpose. However, its structure and the molecular mechanisms remain elusive. Here, we report structures of hGlyT2 in three functional states, including the apo state, the substrate glycine-bound state, and the inhibitor-bound states. The apo state of hGlyT2 adopts an inward conformation. The substrate glycine binds at the central pocket of hGlyT2 in its occluded conformation. Both inhibitors, ORG25543 and opiranserin, bind to an allosteric site, which is vertical to the extracellular tunnel, buried under the extracellular loop 4 (EL4) and near to the transmembrane helix 1b (TM1b). These inhibitors act as wedges to prevent the inward movement of TM1b and closure of the extracellular gate. Further structural analysis reveals both global and local conformational changes associated with the ions and glycine binding and release. These structures define the mechanisms governing transport and allosteric inhibition in hGlyT2, providing a blueprint for further development of non-opioid analgesics targeting hGlyT2.
External linksNat Commun / PubMed:41991951 / PubMed Central
MethodsEM (single particle)
Resolution2.73 - 3.2 Å
Structure data

65747

9w8j

EMDB-65747, PDB-9w8j:
Transport and inhibition mechanisms of human glycine transporter 2
Method: EM (single particle) / Resolution: 2.73 Å

65748

9w8q

EMDB-65748, PDB-9w8q:
Transport and inhibition mechanisms of human glycine transporter 2
Method: EM (single particle) / Resolution: 3.2 Å

65847

9wbr

EMDB-65847, PDB-9wbr:
The structure of glycine transport 2 in apo state
Method: EM (single particle) / Resolution: 3.13 Å

65856

9wc6

EMDB-65856, PDB-9wc6:
The structure of glycine transport 2 in complex with glycine
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

PDB-1ef3:
FIDARESTAT BOUND TO HUMAN ALDOSE REDUCTASE

ChemComp-NA:
Unknown entry

ChemComp-CL:
Unknown entry

PDB-1ef1:
CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX

ChemComp-GLY:
GLYCINE

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / GlyT2 / membrane transport protein / Opiranserin / Glycine transport 2

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