GLUT1

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==Facilitated Glucose Transporter 1, Solute Carrier Family 2, ''Homo sapiens''==
==Facilitated Glucose Transporter 1, Solute Carrier Family 2, ''Homo sapiens''==
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<StructureSection load='4pyp' size='340' side='right' caption='Crystal structure 4PYP from PDB' scene=''>
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<StructureSection load='4pyp' size='340' side='right' caption='Glucose ABC transporter complex with nonyl beta-D-glucopyranoside (PDB code [[4pyp]])' scene=''>
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__TOC__
== Classification ==
== Classification ==
GLUT proteins, encoded by the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4104978/ SLC2] genes, are part of the Major Facilitator Superfamily (MFS) of substrate transporters. Structural elements characteristic of GLUT proteins are twelve transmembrane domains, one N-linked glycosylation site, and lengths of about five-hundred amino acids.<ref>PMID:23506862</ref> GLUT proteins transport a variety of monosaccharides that enable cellular respiration and are thus abundant in the body. Referencing the [http://cathdb.info/version/v4_3_0/superfamily/1.20.1250.20 CATH] classification database, the MFS superfamily has 23,982 unique species and 134 characteristic domains. GLUT1 has two highly-conserved ATP-binding domains known as Walker motifs A and B.<ref>PMID:15326030</ref> A third ATP-binding domain is less conserved. According to [https://www.uniprot.org/uniprot/?query=job:P2022050392C7BAECDB1C5C413EE0E0348724B682005B3CL&columns=id,entry%20name,reviewed,protein%20names,genes,organism,length,peptidesearch(P2022050392C7BAECDB1C5C413EE0E0348724B682005B3CL) UniProt], these specific sequences in the GLUT1 transporter are shared among glucose transporters in several different organisms.
GLUT proteins, encoded by the [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4104978/ SLC2] genes, are part of the Major Facilitator Superfamily (MFS) of substrate transporters. Structural elements characteristic of GLUT proteins are twelve transmembrane domains, one N-linked glycosylation site, and lengths of about five-hundred amino acids.<ref>PMID:23506862</ref> GLUT proteins transport a variety of monosaccharides that enable cellular respiration and are thus abundant in the body. Referencing the [http://cathdb.info/version/v4_3_0/superfamily/1.20.1250.20 CATH] classification database, the MFS superfamily has 23,982 unique species and 134 characteristic domains. GLUT1 has two highly-conserved ATP-binding domains known as Walker motifs A and B.<ref>PMID:15326030</ref> A third ATP-binding domain is less conserved. According to [https://www.uniprot.org/uniprot/?query=job:P2022050392C7BAECDB1C5C413EE0E0348724B682005B3CL&columns=id,entry%20name,reviewed,protein%20names,genes,organism,length,peptidesearch(P2022050392C7BAECDB1C5C413EE0E0348724B682005B3CL) UniProt], these specific sequences in the GLUT1 transporter are shared among glucose transporters in several different organisms.
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__TOC__
 
== Function ==
== Function ==
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There is at least one known amino acid substitution in GLUT1 that can cause GLUT1 deficiency syndrome. <scene name='91/910668/Glut1_arg126_1/1'>Arg126</scene> causes transmembrane helix #4 to become kinked, blocking substrate transport. Arg126 is the amino acid most often mutated in GLUT1 deficiency syndrome.<ref>PMID:18387950</ref>
There is at least one known amino acid substitution in GLUT1 that can cause GLUT1 deficiency syndrome. <scene name='91/910668/Glut1_arg126_1/1'>Arg126</scene> causes transmembrane helix #4 to become kinked, blocking substrate transport. Arg126 is the amino acid most often mutated in GLUT1 deficiency syndrome.<ref>PMID:18387950</ref>
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GLUT1, and other glucose transporters, have an <scene name='91/910668/Ich_domain_1/1'>intracellular helices (ICH) domain</scene>. The ICH domain of GLUT1 may play a role in stabilizing the outward-facing conformation of the enzyme based on computer modeling in [https://en.wikipedia.org/wiki/MODELLER MODELLER].<ref>PMID:25919356</ref> Two residues of interest in the ICH domain are Arg212 and Asp240. These residues are hypothesized to participate in hydrogen bonds between the ICH domain and transmembrane domains of the protein with the cumulative effect of stabilizing the outward-facing conformation.
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GLUT1, and other glucose transporters, have an <scene name='91/910668/Ich_domain_1/1'>intracellular helices (ICH) domain</scene>. The ICH domain of GLUT1 may play a role in stabilizing the outward-facing conformation of the enzyme based on computer modeling in [https://en.wikipedia.org/wiki/MODELLER MODELLER].<ref>PMID:25919356</ref> Two residues of interest in the ICH domain are Arg212 and Asp240. These residues are hypothesized to participate in hydrogen bonding between the ICH domain and transmembrane domains of the protein with the cumulative effect of stabilizing the outward-facing conformation.
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== Summary ==
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GLUT1 is a glucose transporter expressed throughout the body. Increased expression of the protein is noted in tissues such as blood-brain barrier, the placenta, and the retina. GLUT1 works in conjunction with other solute carrier proteins to ensure that metabolically-demanding tissues receive a steady supply of substrates for ATP production. GLUT1 is implicated in a variety of pathologies such as GLUT1 deficiency syndrome, cancer, diabetes, and more. Dozens of studies on GLUT1 structure have revealed domains important in glucose binding and possibly allosteric regulation. Further research is necessary to fully understand GLUT1 function, but progress in biochemistry has provided many clues as to how GLUT1 works.
== References ==
== References ==
<references/>
<references/>

Current revision

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

Glucose ABC transporter complex with nonyl beta-D-glucopyranoside (PDB code 4pyp)

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Adam Kingsley, Michal Harel

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