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 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>
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 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>
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<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_2/2'>(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>
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<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_2/3'>(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>
The GLUT1 transporter also has three proposed ATP-binding sites. The lone <scene name='91/910668/Glut1_atp_binding_1/2'>extracellular ATP-binding site</scene> is proposed to be comprised of the residues Gly111, Phe112, Ser113, Lys114, Leu115, Gly116, Lys117, and Ser118. This is a domain consistent with Walker Motif A (G-X-X-G/X-X-G-K-T/X). The <scene name='91/910668/Glut1_atp_binding_2/2'>second ATP-binding site</scene> is one of two in the cytoplasmic portion of the protein. The residues comprising this ATP-binding site are Lys225, Ser226, Val227, Leu228, and Lys229. The <scene name='91/910668/Atp_binding_site_3/2'>third ATP-binding site</scene>, also localized to the cytoplasm, is comprised of the amino acids Gly332, Arg 333, Arg334, Thr335, Leu336, His337, and Leu338. This sequence is consistent with Walker Motif B (G-X-X-X-L-X-X).<ref>PMID:11425315</ref> Some studies on GLUT1 show that ATP binding to the cytosolic domains causes C-terminus binding to the C-terminal side of the intracellular loop of the protein, preventing substrate import. ATP binding is not known to have any effects when binding extracellularly.<ref>PMID:25715702</ref>
The GLUT1 transporter also has three proposed ATP-binding sites. The lone <scene name='91/910668/Glut1_atp_binding_1/2'>extracellular ATP-binding site</scene> is proposed to be comprised of the residues Gly111, Phe112, Ser113, Lys114, Leu115, Gly116, Lys117, and Ser118. This is a domain consistent with Walker Motif A (G-X-X-G/X-X-G-K-T/X). The <scene name='91/910668/Glut1_atp_binding_2/2'>second ATP-binding site</scene> is one of two in the cytoplasmic portion of the protein. The residues comprising this ATP-binding site are Lys225, Ser226, Val227, Leu228, and Lys229. The <scene name='91/910668/Atp_binding_site_3/2'>third ATP-binding site</scene>, also localized to the cytoplasm, is comprised of the amino acids Gly332, Arg 333, Arg334, Thr335, Leu336, His337, and Leu338. This sequence is consistent with Walker Motif B (G-X-X-X-L-X-X).<ref>PMID:11425315</ref> Some studies on GLUT1 show that ATP binding to the cytosolic domains causes C-terminus binding to the C-terminal side of the intracellular loop of the protein, preventing substrate import. ATP binding is not known to have any effects when binding extracellularly.<ref>PMID:25715702</ref>

Revision as of 22:28, 2 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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