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Structure paper

TitleRole of a noncanonical disulfide bond in the stability, affinity, and flexibility of a VHH specific for the Listeria virulence factor InlB.
Journal, issue, pagesProtein Sci., Vol. 29, Page 1004-1017, Year 2020
Publish dateAug 15, 2019 (structure data deposition date)
AuthorsMendoza, M.N. / Jian, M. / King, M.T. / Brooks, C.L.
External linksProtein Sci. / PubMed:31981247
MethodsX-ray diffraction
Resolution1.3 - 1.56 Å
Structure data

PDB-6u12:
VHH R303 C33A/C102A in complex withthe LRR domain of InlB
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

PDB-6u14:
VHH R303 C33A/C102A in complex withthe LRR domain of InlB
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • listeria monocytogenes (bacteria)
  • camelus dromedarius (Arabian camel)
KeywordsIMMUNE SYSTEM / Nanobody / VHH / Internalin / Listeria / Disulfide bond

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