1H8U

Crystal Structure of the Eosinophil Major Basic Protein at 1.8A: An Atypical Lectin with a Paradigm Shift in Specificity

Summary for 1H8U

• Entry DOI: 10.2210/pdb1h8u/pdb
• Descriptor: EOSINOPHIL GRANULE MAJOR BASIC PROTEIN 1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lectin, eosinophil granule protein, embp
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 2
• Total formula weight: 28594.49

Authors

Swaminathan, G.J.,Weaver, A.J.,Loegering, D.A.,Checkel, J.L.,Leonidas, D.D.,Gleich, G.J.,Acharya, K.R. (deposition date: 2001-02-15, release date: 2001-07-17, Last modification date: 2024-10-23)

Primary citation

Swaminathan, G.J.,Weaver, A.J.,Loegering, D.A.,Checkel, J.L.,Leonidas, D.D.,Gleich, G.J.,Acharya, K.R.
Crystal Structure of the Eosinophil Major Basic Protein at 1.8A. An Atypical Lectin with a Paradigm Shift in Specificity
J.Biol.Chem., 276:26197-, 2001

PubMed Abstract: The eosinophil major basic protein (EMBP) is the predominant constituent of the crystalline core of the eosinophil primary granule. EMBP is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases such as asthma. Here we report the crystal structure of EMBP at 1.8 A resolution, and show that it is similar to that of members of the C-type lectin superfamily with which it shares minimal amino acid sequence identity (approximately 15--28%). However, this protein lacks a Ca(2+)/carbohydrate-binding site. Our analysis suggests that EMBP specifically binds heparin. Based on our results, we propose a possible new function for this protein, which is likely to have implications for EMBP function.

PubMed: 11319227
DOI: 10.1074/JBC.M100848200

Experimental method

X-RAY DIFFRACTION (1.8 Å)