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http://purl.uniprot.org/citations/23702291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23702291http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23702291http://www.w3.org/2000/01/rdf-schema#comment"Very few studies have attributed a direct, active, functional role to N-linked glycans. We describe here an N-linked glycan with a unique role for maintaining the active conformation of a protein of the serpin family. The distinguishing feature of serpins is the "stressed-to-relaxed" transition, in which the reactive center loop inserts as a β-strand into the central β-sheet A. This transition forms the basis for the conversion of serpins to the inactive latent state. We demonstrate that plasminogen activator inhibitor-1 (PAI-1) from zebrafish converts to the latent state about 5-fold slower than human PAI-1. In contrast to human PAI-1, fish PAI-1 carries a single N-linked glycan at Asn185 in the gate region through which the reactive center loop passes during latency transition. While the latency transition of human PAI-1 is unaffected by deglycosylation, deglycosylated zebrafish PAI-1 (zfPAI-1) goes latent about 50-fold faster than the glycosylated zfPAI-1 and about 25-fold faster than non-glycosylated human PAI-1. X-ray crystal structure analysis of glycosylated fish PAI-1 confirmed the presence of an N-linked glycan in the gate region and a lack of glycan-induced structural changes. Thus, latency transition of zfPAI-1 is delayed by steric hindrance from the glycan in the gate region. Our findings reveal a previously unknown mechanism for inhibition of protein conformational changes by steric hindrance from N-linked glycans."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2013.05.007"xsd:string
http://purl.uniprot.org/citations/23702291http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2013.05.007"xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Stensballe A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Stensballe A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Jensen J.K."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Jensen J.K."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Andreasen P.A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Andreasen P.A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Sorensen H.P."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Sorensen H.P."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Johansen J.S."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Johansen J.S."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Jendroszek A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Jendroszek A."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Bager R."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Bager R."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Buxbom L."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/author"Buxbom L."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/23702291http://purl.uniprot.org/core/name"J Mol Biol"xsd:string