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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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

Institucijski repozitorij: Repozitorij Medicinskog fakulteta u Rijeci

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Naschberger, A., Fürnrohr, B. G., Lenac Roviš, T., Malic, S., Scheffzek, K., Dieplinger, H. i 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, br. 12, 2016, str. 1267-1280. https://doi.org/10.1107/S205979831601723X

Naschberger, Andreas, Barbara G. Fürnrohr, Tihana Lenac Roviš, Suzana Malic, Klaus Scheffzek, Hans Dieplinger i 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, br. 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), str. 1267-1280. doi: 10.1107/S205979831601723X

Naschberger A, Fürnrohr BG, Lenac Roviš T, Malic S, Scheffzek K, Dieplinger H, i 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]. 29.11.2016. [pristupljeno 13.05.2024.];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, br. 12, str. 1267-1280, Studeni 2016. [Online]. Dostupno na: https://urn.nsk.hr/urn:nbn:hr:184:910017. [Citirano: 13.05.2024.]

Za citiranje koristite ovu mrežnu adresu: https://urn.nsk.hr/urn:nbn:hr:184:910017
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Naslov (engleski)The N14 anti-afamin antibody Fab: a rare V 1 CDR glycosylation, crystallographic re-sequencing, molecular plasticity and conservative enthusiastic modelling
AutorAndreas Naschberger
AutorBarbara G. Fürnrohr
AutorTihana Lenac Roviš
AutorSuzana Malic
AutorKlaus Scheffzek
AutorHans Dieplinger
AutorBernhard Rupp
Autorova ustanovaSveučilište u Rijeci
Medicinski fakultet
(Centar za proteomiku)
Znanstveno / umjetničko
područje, polje i grana		BIOMEDICINA I ZDRAVSTVO
Temeljne medicinske znanosti
Sažetak (engleski)
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.
Ključne riječi (engleski)
Jezikengleski
Vrsta publikacijeZnanstveni rad - Izvorni znanstveni rad
Status objaveObjavljen
Vrsta recenzijeRecenziran - međunarodna recenzija
Verzija publikacijeObjavljena verzija rada (izdavačev PDF)
Naslov časopisaActa Crystallographica Section D Structural Biology
Brojčani podacivol. 72, br. 12, str. 1267-1280
p-ISSN2059-7983
DOIhttps://doi.org/10.1107/S205979831601723X
URN:NBNurn:nbn:hr:184:910017
Datum objave publikacije2016-11-29
Datum objave publikacije2016-12-01
URL dokumentahttp://scripts.iucr.org/cgi-bin/paper?S205979831601723X
Vrsta resursaTekst
Prava pristupaOtvoreni pristup
Uvjeti korištenjaIkona licence Zaštićeno autorskim pravom.
Datum i vrijeme pohrane2018-11-05 14:18:00