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Article

The biological assembly of OXA-48 reveals a dimer interface with high charge complementarity and very high affinity.

The FEBS journal - 1 Nov 2018

Lund Bjarte Aarmo, Thomassen Ane Molden, Nesheim Birgit Helene Berg, Carlsen Trine Josefine Olsen, Isaksson Johan, Christopeit Tony, Leiros Hanna-Kirsti S

Abstract excerpt

Many class D β-lactamases form dimers in solution. The functional basis of the dimerization of OXA-48-like class D β-lactamases is not known, but in order to understand the structural requirements for dimerization of OXA-48, we have characterized the dimer interface. Size exclusion chromatography, small angle X-ray scattering (SAXS), and nuclear magnetic resonance (NMR) were used to confirm the oligomeric state...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 30153368
DOI: 10.1111/febs.14643

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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