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http://purl.uniprot.org/citations/26176916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26176916http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26176916http://www.w3.org/2000/01/rdf-schema#comment"The major facilitator superfamily glucose transporters, exemplified by human GLUT1-4, have been central to the study of solute transport. Using lipidic cubic phase crystallization and microfocus X-ray diffraction, we determined the structure of human GLUT3 in complex with D-glucose at 1.5 Å resolution in an outward-occluded conformation. The high-resolution structure allows discrimination of both α- and β-anomers of D-glucose. Two additional structures of GLUT3 bound to the exofacial inhibitor maltose were obtained at 2.6 Å in the outward-open and 2.4 Å in the outward-occluded states. In all three structures, the ligands are predominantly coordinated by polar residues from the carboxy terminal domain. Conformational transition from outward-open to outward-occluded entails a prominent local rearrangement of the extracellular part of transmembrane segment TM7. Comparison of the outward-facing GLUT3 structures with the inward-open GLUT1 provides insights into the alternating access cycle for GLUTs, whereby the C-terminal domain provides the primary substrate-binding site and the amino-terminal domain undergoes rigid-body rotation with respect to the C-terminal domain. Our studies provide an important framework for the mechanistic and kinetic understanding of GLUTs and shed light on structure-guided ligand design."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.org/dc/terms/identifier"doi:10.1038/nature14655"xsd:string
http://purl.uniprot.org/citations/26176916http://purl.org/dc/terms/identifier"doi:10.1038/nature14655"xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Jiang X."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Jiang X."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Ren W."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Ren W."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yamamoto M."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Hirata K."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Hirata K."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Sun P."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Sun P."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Deng D."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Deng D."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yan C."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yan C."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Xiong L."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Xiong L."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Fan S."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Fan S."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yan N."xsd:string
http://purl.uniprot.org/citations/26176916http://purl.uniprot.org/core/author"Yan N."xsd:string