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Structure paper

TitleBinding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation.
Journal, issue, pagesMol. Microbiol., Vol. 67, Page 420-434, Year 2008
Publish dateJul 31, 2007 (structure data deposition date)
AuthorsKorotkova, N. / Yang, Y. / Le Trong, I. / Cota, E. / Demeler, B. / Marchant, J. / Thomas, W.E. / Stenkamp, R.E. / Moseley, S.L. / Matthews, S.
External linksMol. Microbiol. / PubMed:18086185
MethodsX-ray diffraction / NMR (solution)
Resolution1.95 - 2.9 Å
Structure data

PDB-2qsq:
Crystal structure of the N-terminal domain of carcinoembryonic antigen (CEA)
Method: X-RAY DIFFRACTION / Resolution: 1.95 Å

PDB-2qst:
Crystal structure of the V39C mutant of the N-terminal domain of carcinoembryonic antigen (CEA)
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-2ver:
Structural model for the complex between the Dr adhesins and carcinoembryonic antigen (CEA)
Method: SOLUTION NMR

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-MTN:
S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate

Source
  • homo sapiens (human)
  • escherichia coli (E. coli)
KeywordsCELL ADHESION / Glycoprotein / GPI-anchor / Immunoglobulin domain / Lipoprotein / Membrane / Polymorphism / FIMBRIUM / CELL PROJECTION

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