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TitleStructural mechanism of SGLT1 inhibitors.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6440, Year 2022
Publish dateOct 28, 2022
AuthorsYange Niu / Wenhao Cui / Rui Liu / Sanshan Wang / Han Ke / Xiaoguang Lei / Lei Chen /
PubMed AbstractSodium glucose co-transporters (SGLT) harness the electrochemical gradient of sodium to drive the uphill transport of glucose across the plasma membrane. Human SGLT1 (hSGLT1) plays a key role in ...Sodium glucose co-transporters (SGLT) harness the electrochemical gradient of sodium to drive the uphill transport of glucose across the plasma membrane. Human SGLT1 (hSGLT1) plays a key role in sugar uptake from food and its inhibitors show promise in the treatment of several diseases. However, the inhibition mechanism for hSGLT1 remains elusive. Here, we present the cryo-EM structure of the hSGLT1-MAP17 hetero-dimeric complex in the presence of the high-affinity inhibitor LX2761. LX2761 locks the transporter in an outward-open conformation by wedging inside the substrate-binding site and the extracellular vestibule of hSGLT1. LX2761 blocks the putative water permeation pathway of hSGLT1. The structure also uncovers the conformational changes of hSGLT1 during transitions from outward-open to inward-open states.
External linksNat Commun / PubMed:36307403 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

32617

7wmv

EMDB-32617, PDB-7wmv:
Structure of human SGLT1-MAP17 complex bound with LX2761
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-1YI:
N-[2-(dimethylamino)ethyl]-2-methyl-2-[4-[4-[[2-methyl-5-[(2S,3R,4R,5S,6R)-6-methylsulfanyl-3,4,5-tris(oxidanyl)oxan-2-yl]phenyl]methyl]phenyl]butanoylamino]propanamide

Source
  • homo sapiens (human)
KeywordsPROTEIN TRANSPORT / glucose transporter / SGLT / sodium glucose transporter / membrane protein

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