GLUT1

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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. Varied molecular weights of the GLUT1 transporter suggest glycosylation is dependent on cell type. This glycosylation site is thought to be important for increasing 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 increase the Km of the enzyme.<ref>PMID:1761560</ref> In addition, samples of both bovine capillaries and choroid plexus cells show differences in GLUT1 molecular weight attributable to N-linked glycosylation.<ref>PMID:8038191</ref> This evidence suggests that GLUT1 glycosylation may differ by tissue type to serve certain functions.
The GLUT1 transporter has one known <scene name='91/910668/Glut1_n-glycosylation/1'>N-linked glycosylation</scene> site at Asn 45. Varied molecular weights of the GLUT1 transporter suggest glycosylation is dependent on cell type. This glycosylation site is thought to be important for increasing 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 increase the Km of the enzyme.<ref>PMID:1761560</ref> In addition, samples of both bovine capillaries and choroid plexus cells show differences in GLUT1 molecular weight attributable to N-linked glycosylation.<ref>PMID:8038191</ref> This evidence suggests that GLUT1 glycosylation may differ by tissue type to serve certain functions.
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GLUT1 and [[Glut3]] have a <scene name='91/910668/Glut1_conformational_change_1/1'>two shared motifs</scene> that are predicted to stabilize the "outward" conformation of both proteins, allowing extracellular glucose binding.<ref>PMID:33536238</ref> The implications of this finding are that these two motifs may play a key role in conformational changes involved in glucose import.
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GLUT1 and [[Glut3]] have a <scene name='91/910668/Glut1_conformational_change_1/1'>two shared motifs</scene> that are predicted to stabilize the "outward" conformation of both proteins, allowing extracellular glucose binding.<ref>PMID:33536238</ref> These motifs are referred to as the "A" and "SP" motifs. The implications of this finding are that these two motifs may play a key role in conformational changes involved in glucose import. The sequence of the A motif, from residue 84 to residue 93, is G-L-F-V-N-R-F-G-R-R. The sequence of the SP motif, from residue 208 to residue 212, is P-E-S-P-R.
<scene name='91/910668/Glut1_default_view_charged/1'>GLUT1</scene> has a <scene name='91/910668/Glut1_hydrophobic_pocket/1'>hydrophobic pocket</scene> and is proposed to be comprised of <scene name='91/910668/Glut1_hps_2/1'>six amino acids</scene><scene name='91/910668/Glut1_hps_2/5'>(view 2)</scene>. In the structure [[4pyp]], these residues are Gly27, Thr30, Ile164, Val165, Ile168, and Phe291. This hydrophobic pocket has been proposed to facilitate substrate binding and unbinding between the "occluded" and "inward-open" conformations.<ref>PMID:27128978</ref> In this crystal structure, <scene name='91/910668/B-ng_in_4pyp/1'>N-nonyl-β-D-glucopyranoside (β-NG)</scene> acts as a glucose analog that binds the hydrophobic pocket.<ref>PMID:24847886</ref>
<scene name='91/910668/Glut1_default_view_charged/1'>GLUT1</scene> has a <scene name='91/910668/Glut1_hydrophobic_pocket/1'>hydrophobic pocket</scene> and is proposed to be comprised of <scene name='91/910668/Glut1_hps_2/1'>six amino acids</scene><scene name='91/910668/Glut1_hps_2/5'>(view 2)</scene>. In the structure [[4pyp]], these residues are Gly27, Thr30, Ile164, Val165, Ile168, and Phe291. This hydrophobic pocket has been proposed to facilitate substrate binding and unbinding between the "occluded" and "inward-open" conformations.<ref>PMID:27128978</ref> In this crystal structure, <scene name='91/910668/B-ng_in_4pyp/1'>N-nonyl-β-D-glucopyranoside (β-NG)</scene> acts as a glucose analog that binds the hydrophobic pocket.<ref>PMID:24847886</ref>

Revision as of 01:47, 3 May 2022

Facilitated Glucose Transporter 1, Solute Carrier Family 2, Homo sapiens

Crystal structure 4PYP from PDB

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Proteopedia Page Contributors and Editors (what is this?)

Adam Kingsley, Michal Harel

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