prikaz prve stranice dokumenta The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling
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Scientific paper - Original scientific paper
The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling
Acta Crystallographica Section D Structural Biology, 72 (2016), 12; 1267-1280. https://doi.org/10.1107/S205979831601723X
Naschberger, Andreas; Fürnrohr, Barbara G.; Lenac Roviš, Tihana; Malic, Suzana; Scheffzek, Klaus; Dieplinger, Hans; Rupp, Bernhard

Institutional repository: Repository of the University of Rijeka, Faculty of Medicine

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Naschberger, A., Fürnrohr, B. G., Lenac Roviš, T., Malic, S., Scheffzek, K., Dieplinger, H. & Rupp, B. (2016). The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling. Acta Crystallographica Section D Structural Biology, 72. (12), 1267-1280. doi: 10.1107/S205979831601723X

Naschberger, Andreas, et al. "The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling." Acta Crystallographica Section D Structural Biology, vol. 72, no. 12, 2016, pp. 1267-1280. https://doi.org/10.1107/S205979831601723X

Naschberger, Andreas, Barbara G. Fürnrohr, Tihana Lenac Roviš, Suzana Malic, Klaus Scheffzek, Hans Dieplinger and Bernhard Rupp. "The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling." Acta Crystallographica Section D Structural Biology 72, no. 12 (2016): 1267-1280. https://doi.org/10.1107/S205979831601723X

Naschberger, A., et al. (2016) 'The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling', Acta Crystallographica Section D Structural Biology, 72(12), pp. 1267-1280. doi: 10.1107/S205979831601723X

Naschberger A, Fürnrohr BG, Lenac Roviš T, Malic S, Scheffzek K, Dieplinger H, and sur.. The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling. Acta Crystallographica Section D Structural Biology [Internet]. 2016 November 29 [cited 2024 May 16];72(12):1267-1280. doi: 10.1107/S205979831601723X

A. Naschberger, et al., "The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling", Acta Crystallographica Section D Structural Biology, vol. 72, no. 12, pp. 1267-1280, November 2016. [Online]. Available at: https://urn.nsk.hr/urn:nbn:hr:184:910017. [Accessed: 16 May 2024]

Metadata
Title (english)The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling
AuthorAndreas Naschberger
AuthorBarbara G. Fürnrohr
AuthorTihana Lenac Roviš
AuthorSuzana Malic
AuthorKlaus Scheffzek
AuthorHans Dieplinger
AuthorBernhard Rupp
Author's institutionUniversity of Rijeka
Faculty of Medicine
(Center for Proteomics)
Scientific / art field,
discipline and subdiscipline		BIOMEDICINE AND HEALTHCARE
Basic Medical Sciences
Abstract (english)
The monoclonal antibody N14 is used as a detection antibody in ELISA kits for the human glycoprotein afamin, a member of the albumin family, which has recently gained interest in the capture and stabilization of Wnt signalling proteins, and for its role in metabolic syndrome and papillary thyroid carcinoma. As a rare occurrence, the N14 Fab is N-glycosylated at Asn26L at the onset of the V 1 antigen-binding loop, with the α-1–6 core fucosylated complex glycan facing out of the L1 complementarity-determining region. The crystal structures of two non-apparent (pseudo) isomorphous crystals of the N14 Fab were analyzed, which differ significantly in the elbow angles, thereby cautioning against the overinterpretation of domain movements upon antigen binding. In addition, the map quality at 1.9 Å resolution was sufficient to crystallographically re-sequence the variable V and V domains and to detect discrepancies in the hybridoma-derived sequence. Finally, a conservatively refined parsimonious model is presented and its statistics are compared with those from a less conservatively built model that has been modelled more enthusiastically. Improvements to the PDB validation reports affecting ligands, clashscore and buried surface calculations are suggested.
Keywords (english)
Languageenglish
Publication typeScientific paper - Original scientific paper
Publication statusPublished
Peer reviewPeer review - international
Publication versionPublished version
Journal titleActa Crystallographica Section D Structural Biology
Numberingvol. 72, no. 12, pp. 1267-1280
p-ISSN2059-7983
DOIhttps://doi.org/10.1107/S205979831601723X
URN:NBNurn:nbn:hr:184:910017
Publication2016-11-29
Publication2016-12-01
Document URLhttp://scripts.iucr.org/cgi-bin/paper?S205979831601723X
Type of resourceText
Access conditionsOpen access
Terms of useLicence In copyright icon
Created on2018-11-05 14:18:00