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Structure paper

TitleStructural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
Journal, issue, pagesFront Immunol, Vol. 10, Page 2007-2007, Year 2019
Publish dateMay 27, 2019 (structure data deposition date)
AuthorsPedersen, D.V. / Gadeberg, T.A.F. / Thomas, C. / Wang, Y. / Joram, N. / Jensen, R.K. / Mazarakis, S.M.M. / Revel, M. / El Sissy, C. / Petersen, S.V. ...Pedersen, D.V. / Gadeberg, T.A.F. / Thomas, C. / Wang, Y. / Joram, N. / Jensen, R.K. / Mazarakis, S.M.M. / Revel, M. / El Sissy, C. / Petersen, S.V. / Lindorff-Larsen, K. / Thiel, S. / Laursen, N.S. / Fremeaux-Bacchi, V. / Andersen, G.R.
External linksFront Immunol / PubMed:31507604
MethodsX-ray diffraction
Resolution1.26 - 6.15 Å
Structure data

PDB-6ru3:
Crystal structure of the FP specific nanobody hFPNb1
Method: X-RAY DIFFRACTION / Resolution: 1.26 Å

PDB-6ru5:
human complement C3 in complex with the hC3Nb1 nanobody
Method: X-RAY DIFFRACTION / Resolution: 3.9 Å

PDB-6rur:
Structure of the SCIN stabilized C3bBb convertase bound to properdin
Method: X-RAY DIFFRACTION / Resolution: 6 Å

PDB-6rus:
Structure of a functional properdin monomer
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-6ruv:
Structure of the SCIN stabilized C3bBb convertase bound to Properdin and a the non-inhibitory nanobody hFPNb1
Method: X-RAY DIFFRACTION / Resolution: 6.15 Å

PDB-6rv6:
Structure of properdin lacking TSR3 based on anomalous data
Method: X-RAY DIFFRACTION / Resolution: 3.507 Å

PDB-6sej:
Structure of a functional monomeric properdin lacking TSR3
Method: X-RAY DIFFRACTION / Resolution: 3.501 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-MAN:
alpha-D-mannopyranose

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

Source
  • lama glama (llama)
  • homo sapiens (human)
  • staphylococcus aureus (bacteria)
KeywordsIMMUNE SYSTEM / antibody / nanobody / single domain antibody / innate immunity / complement C3 / complement / protease / regulator / proteolytic enzyme

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