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GLUT1

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== Structural highlights ==
== Structural highlights ==
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The GLUT1 transporter has one known <scene name='91/910668/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45. This glycosylation site is thought to be important for glucose binding to the extracellular portion of the transporter. Mutations in the GLUT1 transporter from Asn 45 to an Asp, Tyr, or Gln residue have been shown to decrease the [[Km]] of the enzyme.<ref>PMID:1761560</ref>
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The GLUT1 transporter has one known <scene name='91/910668/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45. This glycosylation site is thought to be important for glucose binding to the extracellular portion of the transporter. Mutations in the GLUT1 transporter from Asn 45 to an Asp, Tyr, or Gln residue have been shown to decrease the Km of the enzyme.<ref>PMID:1761560</ref>
</StructureSection>
</StructureSection>
== References ==
== References ==
Asano T, Katagiri H, Takata K, Lin JL, Ishihara H, Inukai K, Tsukuda K, Kikuchi M, Hirano H, Yazaki Y, et al. The role of N-glycosylation of GLUT1 for glucose transport activity. J Biol Chem. 1991 Dec 25;266(36):24632-6. PMID: 1761560.
Asano T, Katagiri H, Takata K, Lin JL, Ishihara H, Inukai K, Tsukuda K, Kikuchi M, Hirano H, Yazaki Y, et al. The role of N-glycosylation of GLUT1 for glucose transport activity. J Biol Chem. 1991 Dec 25;266(36):24632-6. PMID: 1761560.

Revision as of 19:03, 25 April 2022

Structure

Caption for this structure

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References

Asano T, Katagiri H, Takata K, Lin JL, Ishihara H, Inukai K, Tsukuda K, Kikuchi M, Hirano H, Yazaki Y, et al. The role of N-glycosylation of GLUT1 for glucose transport activity. J Biol Chem. 1991 Dec 25;266(36):24632-6. PMID: 1761560.

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