Matches in Ghent University Academic Bibliography for { <https://biblio.ugent.be/publication/01GMVB1YBQR1WEH9WHEXKSJDZB> ?p ?o. }
Showing items 1 to 20 of
20
with 100 items per page.
- 01GMVB1YBQR1WEH9WHEXKSJDZB classification C3.
- 01GMVB1YBQR1WEH9WHEXKSJDZB date "2022".
- 01GMVB1YBQR1WEH9WHEXKSJDZB language "eng".
- 01GMVB1YBQR1WEH9WHEXKSJDZB type conference.
- 01GMVB1YBQR1WEH9WHEXKSJDZB hasPart 01GMXMMT45612VP62A66XBRNY5.pdf.
- 01GMVB1YBQR1WEH9WHEXKSJDZB subject "Biology and Life Sciences".
- 01GMVB1YBQR1WEH9WHEXKSJDZB subject "Technology and Engineering".
- 01GMVB1YBQR1WEH9WHEXKSJDZB doi "10.5281/zenodo.7400564".
- 01GMVB1YBQR1WEH9WHEXKSJDZB presentedAt urn:uuid:a4135789-c12e-4e1b-b6b8-760d3ca07705.
- 01GMVB1YBQR1WEH9WHEXKSJDZB abstract "Abstract: α-1 Acid glycoprotein (AGP) is one of the most abundant plasma proteins. It fulfills two essential functions: immunomodulation, and binding to various drugs. These different functions are closely associated with each other via changes in the glycosylation of AGP in response to inflammation. From a structural point of view, glycans alter the local biophysical properties of the AGP leading to a diverse ligand-binding spectrum. There is evidence that the AGP's glycosylation can be utilized as a potential biomarker for the prognosis of cancer. However, the resolved X-ray crystallography structure of AGP does not contain glycans, which are not observed due to their high flexibility and microheterogeneity. Thus, it limits our understanding of AGP's conformational dynamics 70 years after its discovery. Also, no studies have linked the effect of AGP glycosylation to cancer missense mutations. Here, we investigate the conformational dynamics of AGP with respect to missense mutations and their effect on glycosylated and un-glycosylated forms of AGP by using Molecular Dynamics (MD) simulation, and sequence-based dynamics predictions. The MD trajectories show that glycosylation decreases the local backbone flexibility of AGP and increases the flexibility of distant regions due to allosteric effects. Moreover, glycosylation compacts the backbone slightly and shields the protein surface reducing its accessibility. We observe that when a residue is mutated close to the glycosylation site, glycan's conformational preferences are affected. Thus, we conclude that mutations control glycan dynamics, which modulates the protein's backbone flexibility directly affecting its accessibility.".
- 01GMVB1YBQR1WEH9WHEXKSJDZB author 7735D764-B25E-11E6-B104-2D2FD0AF0289.
- 01GMVB1YBQR1WEH9WHEXKSJDZB author F7F4F4A2-F0ED-11E1-A9DE-61C894A0A6B4.
- 01GMVB1YBQR1WEH9WHEXKSJDZB author bb54460f-1a3a-11eb-af9f-e38f051f127b.
- 01GMVB1YBQR1WEH9WHEXKSJDZB dateCreated "2022-12-21T21:57:26Z".
- 01GMVB1YBQR1WEH9WHEXKSJDZB dateModified "2024-07-09T07:42:08Z".
- 01GMVB1YBQR1WEH9WHEXKSJDZB name "Dissecting conformational dynamics of α-1 acid glycoprotein (AGP) : a study of glycosylated and un-glycosylated mutants".
- 01GMVB1YBQR1WEH9WHEXKSJDZB pagination urn:uuid:8fdb5b9a-918a-4554-b9ce-c50ec6840b37.
- 01GMVB1YBQR1WEH9WHEXKSJDZB sameAs LU-01GMVB1YBQR1WEH9WHEXKSJDZB.
- 01GMVB1YBQR1WEH9WHEXKSJDZB sourceOrganization urn:uuid:53493995-ddfc-49f2-bee4-552bdd0b170c.
- 01GMVB1YBQR1WEH9WHEXKSJDZB type C3.