| http://purl.uniprot.org/citations/33825709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/33825709 | http://www.w3.org/2000/01/rdf-schema#comment | "The canonical O-mannosylation pathway in humans is essential for the functional glycosylation of α-dystroglycan. Disruption of this post-translational modification pathway leads to congenital muscular dystrophies. The first committed step in the construction of a functional matriglycan structure involves the post-translational modification of α-dystroglycan. This is essential for binding extracellular matrix proteins and arenaviruses, and is catalyzed by β-1,4-N-acetylglucosaminyltransferase 2 (POMGNT2). While another glycosyl transferase, β-1,4-N-acetylglucosaminyltransferase 1 (POMGNT1), has been shown to be promiscuous in extending O-mannosylated sites, POMGNT2 has been shown to display significant primary amino-acid selectivity near the site of O-mannosylation. Moreover, several single point mutations in POMGNT2 have been identified in patients with assorted dystroglycanopathies such as Walker-Warburg syndrome and limb girdle muscular dystrophy. To gain insight into POMGNT2 function in humans, the enzyme was expressed as a soluble, secreted fusion protein by transient infection of HEK293 suspension cultures. Here, crystal structures of POMGNT2 (amino-acid residues 25-580) with and without UDP bound are reported. Consistent with a novel fold and a unique domain organization, no molecular-replacement model was available and phases were obtained through crystallization of a selenomethionine variant of the enzyme in the same space group. Tetragonal (space group P4212; unit-cell parameters a = b = 129.8, c = 81.6 Å, α = γ = β = 90°) crystals with UDP bound diffracted to 1.98 Å resolution and contained a single monomer in the asymmetric unit. Orthorhombic (space group P212121; unit-cell parameters a = 142.3, b = 153.9, c = 187.4 Å, α = γ = β = 90°) crystals were also obtained; they diffracted to 2.57 Å resolution and contained four monomers with differential glycosylation patterns and conformations. These structures provide the first rational basis for an explanation of the loss-of-function mutations and offer significant insights into the mechanics of this important human enzyme."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.org/dc/terms/identifier | "doi:10.1107/s2059798321001261"xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Wells L."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Lanzilotta W.N."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Moremen K.W."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Singh D."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Yang J.Y."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Praissman J."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Chapla D."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/author | "Halmo S.M."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/date | "2021"xsd:gYear |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/name | "Acta Crystallogr D Struct Biol"xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/pages | "486-495"xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/title | "Crystal structures of beta-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies."xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://purl.uniprot.org/core/volume | "77"xsd:string |
| http://purl.uniprot.org/citations/33825709 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/33825709 |
| http://purl.uniprot.org/citations/33825709 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/33825709 |
| http://purl.uniprot.org/uniprot/#_Q8NAT1-mappedCitation-33825709 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/33825709 |
| http://purl.uniprot.org/uniprot/Q8NAT1 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/33825709 |