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Structure paper

TitleStructural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 110, Page 13916-13920, Year 2013
Publish dateJul 10, 2013 (structure data deposition date)
AuthorsVenkatraman Girija, U. / Gingras, A.R. / Marshall, J.E. / Panchal, R. / Sheikh, M.A. / Gal, P. / Schwaeble, W.J. / Mitchell, D.A. / Moody, P.C. / Wallis, R.
External linksProc. Natl. Acad. Sci. USA / PubMed:23922389
MethodsX-ray diffraction
Resolution1.996 - 2.921 Å
Structure data

PDB-4lmf:
C1s CUB1-EGF-CUB2
Method: X-RAY DIFFRACTION / Resolution: 2.921 Å

PDB-4lor:
C1s CUB1-EGF-CUB2 in complex with a collagen-like peptide from C1q
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-4los:
C1s CUB2-CCP1
Method: X-RAY DIFFRACTION / Resolution: 1.996 Å

PDB-4lot:
C1s CUB2-CCP1-CCP2
Method: X-RAY DIFFRACTION / Resolution: 2.92 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-CA:
Unknown entry

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

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / CUB domain / EGF-like domain / Complement C1s / HYDROLASE/protein binding / protein collagen complex / C1 complex / HYDROLASE-protein binding complex / CCP domain

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