GLUT1: Difference between revisions

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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> 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>

Several types of GLUT1 inhibitors exist, one being cytochalasin b. Two Trp residues, Trp388 and Trp412, are thought to play a major role in <scene name='91/910668/Glut1_cytochalasin_b_1/1'>cytochalasin b binding to GLUT1</scene> via hydrophobic interactions.<ref>PMID:7078104</ref>

Several types of GLUT1 inhibitors exist, one being cytochalasin b[https://en.wikipedia.org/wiki/Cytochalasin_B]. Two Trp residues, Trp388 and Trp412, are thought to play a major role in <scene name='91/910668/Glut1_cytochalasin_b_1/1'>cytochalasin b binding to GLUT1</scene> via hydrophobic interactions.<ref>PMID:7078104</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> 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>
-Several types of GLUT1 inhibitors exist, one being cytochalasin b. Two Trp residues, Trp388 and Trp412, are thought to play a major role in <scene name='91/910668/Glut1_cytochalasin_b_1/1'>cytochalasin b binding to GLUT1</scene> via hydrophobic interactions.<ref>PMID:7078104</ref>
+Several types of GLUT1 inhibitors exist, one being cytochalasin b[https://en.wikipedia.org/wiki/Cytochalasin_B]. Two Trp residues, Trp388 and Trp412, are thought to play a major role in <scene name='91/910668/Glut1_cytochalasin_b_1/1'>cytochalasin b binding to GLUT1</scene> via hydrophobic interactions.<ref>PMID:7078104</ref>
 == References ==
 <references/>