GLUT1

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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>
<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>
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The GLUT1 transporter also has three proposed ATP-binding sites. The lone <scene name='91/910668/Glut1_atp_binding_1/1'>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_2/1'>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_3/1'>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>
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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>
== References ==
== References ==
<references/>
<references/>

Revision as of 17:41, 29 April 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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