4R9T

L-ficolin complexed to sulphates

Summary for 4R9T

• Entry DOI: 10.2210/pdb4r9t/pdb
• Related: 2J0G 2J0H 2J0Y 2J3O 4R9J
• Descriptor: Ficolin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ACETATE ION, ... (6 entities in total)
• Functional Keywords: fibrinogen-like domain, innate immunity, pattern recognition protein, lectin, immunology, lectin-like, sugar binding protein, plasma, extracellular
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 75223.09

Authors

Laffly, E.,Lacroix, M.,Martin, L.,Vassal-Stermann, E.,Thielens, N.,Gaboriaud, C. (deposition date: 2014-09-08, release date: 2014-11-05, Last modification date: 2020-07-29)

Primary citation

Laffly, E.,Lacroix, M.,Martin, L.,Vassal-Stermann, E.,Thielens, N.M.,Gaboriaud, C.
Human ficolin-2 recognition versatility extended: An update on the binding of ficolin-2 to sulfated/phosphated carbohydrates.
Febs Lett., 588:4694-4700, 2014

PubMed Abstract: Ficolin-2 has been reported to bind to DNA and heparin, but the mechanism involved has not been thoroughly investigated. X-ray studies of the ficolin-2 fibrinogen-like domain in complex with several new ligands now show that sulfate and phosphate groups are prone to bind to the S3 binding site of the protein. Composed of Arg132, Asp133, Thr136 and Lys221, the S3 site was previously shown to mainly bind N-acetyl groups. Furthermore, DNA and heparin compete for binding to ficolin-2. Mutagenesis studies reveal that Arg132, and to a lesser extent Asp133, are important for this binding property. The versatility of the S3 site in binding N-acetyl, sulfate and phosphate groups is discussed through comparisons with homologous fibrinogen-like recognition proteins.

PubMed: 25447524
DOI: 10.1016/j.febslet.2014.10.042

Experimental method

X-RAY DIFFRACTION (2.25 Å)