Making glycoproteins a little bit sweeter with PDB-REDO.

Autor: van Beusekom B; Division of Biochemistry, Netherlands Cancer Insitute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands., Lütteke T; Institute of Veterinary Physiology and Biochemistry, Justus-Liebig-University Giessen, Frankfurter Strasse 100, 35392 Giessen, Germany., Joosten RP; Division of Biochemistry, Netherlands Cancer Insitute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Jazyk: angličtina
Zdroj: Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2018 Aug 01; Vol. 74 (Pt 8), pp. 463-472. Date of Electronic Publication: 2018 Jul 26.
DOI: 10.1107/S2053230X18004016
Abstrakt: Glycosylation is one of the most common forms of protein post-translational modification, but is also the most complex. Dealing with glycoproteins in structure model building, refinement, validation and PDB deposition is more error-prone than dealing with nonglycosylated proteins owing to limitations of the experimental data and available software tools. Also, experimentalists are typically less experienced in dealing with carbohydrate residues than with amino-acid residues. The results of the reannotation and re-refinement by PDB-REDO of 8114 glycoprotein structure models from the Protein Data Bank are analyzed. The positive aspects of 3620 reannotations and subsequent refinement, as well as the remaining challenges to obtaining consistently high-quality carbohydrate models, are discussed.
(open access.)
Databáze: MEDLINE
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