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Structure paper

TitleE-Selectin Ligand Complexes Adopt an Extended High-Affinity Conformation.
Journal, issue, pagesJ. Mol. Cell. Biol., Vol. 8, Page 62-, Year 2016
Publish dateAug 9, 2013 (structure data deposition date)
AuthorsPreston, R.C. / Jakob, R.P. / Binder, F.P. / Sager, C.P. / Ernst, B. / Maier, T.
External linksJ. Mol. Cell. Biol. / PubMed:26117840
MethodsX-ray diffraction
Resolution1.93 - 2.41 Å
Structure data

PDB-4c16:
E-selectin lectin, EGF-like and two SCR domains complexed with glycomimetic antagonist
Method: X-RAY DIFFRACTION / Resolution: 1.93 Å

PDB-4csy:
E-selectin lectin, EGF-like and two SCR domains complexed with Sialyl Lewis X
Method: X-RAY DIFFRACTION / Resolution: 2.41 Å

Chemicals

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

ChemComp-CA:
Unknown entry

ChemComp-4WC:
(S)-CYCLOHEXYL LACTIC ACID

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-Q6Z:
(1R,2R,3S)-3-methylcyclohexane-1,2-diol

ChemComp-FUC:
alpha-L-fucopyranose

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCELL ADHESION / CELL-ADHESION MOLECULE / C-TYPE LECTIN / INFLAMMATION / LEUKOCYTE / GLYCOMIMETIC / ANTAGONIST / CATCH- BOND / CELL-ADHESION / HUMAN LECTIN / SIALYL LEWIS X / SLEX / PROTEIN CONFORMATION / LIGAND-INDUCED CONFORMATIONAL CHANGE

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