2BRS

EMBP Heparin complex

Summary for 2BRS

• Entry DOI: 10.2210/pdb2brs/pdb
• Related: 1H8U
• Descriptor: EOSINOPHIL-GRANULE MAJOR BASIC PROTEIN, 2-O-sulfo-beta-L-altropyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: antibiotic, embp, eosinophil, eosinophil granule protein, glycoprotein, heparin-binding, immune response, lectin, proteoglycan, heparin
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Bone marrow proteoglycan: Secreted. Eosinophil granule major basic protein: Cytoplasmic vesicle, secretory vesicle: P13727
• Total number of polymer chains: 2
• Total formula weight: 29005.79

Authors

Swaminathan, G.J.,Myszka, D.G.,Katsamba, P.S.,Ohnuki, L.E.,Gleich, G.J.,Acharya, K.R. (deposition date: 2005-05-11, release date: 2005-10-26, Last modification date: 2024-10-16)

Primary citation

Swaminathan, G.J.,Myszka, D.G.,Katsamba, P.S.,Ohnuki, L.E.,Gleich, G.J.,Acharya, K.R.
Eosinophil-Granule Major Basic Protein, a C-Type Lectin, Binds Heparin
Biochemistry, 44:14152-, 2005

PubMed Abstract: The eosinophil major basic protein (EMBP), a constituent of the eosinophil secondary granule, is implicated in cytotoxicity and mediation of allergic disorders such as asthma. It is a member of the C-type lectin family, but lacks a Ca(2+)- and carbohydrate-binding site as seen in other members of this family. Here, we report the crystal structure of EMBP in complex with a heparin disaccharide and in the absence of Ca(2+), the first such report of any C-lectin with this sugar. We also provide direct evidence of binding of EMBP to heparin and heparin disaccharide by surface plasmon resonance. We propose that the sugars recognized by EMBP are likely to be proteoglycans such as heparin, leading to new interpretations for EMBP function.

PubMed: 16245931
DOI: 10.1021/BI051112B

Experimental method

X-RAY DIFFRACTION (2.2 Å)