1H8U

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

1H8U の概要

• エントリーDOI: 10.2210/pdb1h8u/pdb
• 分子名称: EOSINOPHIL GRANULE MAJOR BASIC PROTEIN 1, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: lectin, eosinophil granule protein, embp
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28594.49

構造登録者

Swaminathan, G.J.,Weaver, A.J.,Loegering, D.A.,Checkel, J.L.,Leonidas, D.D.,Gleich, G.J.,Acharya, K.R. (登録日: 2001-02-15, 公開日: 2001-07-17, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.8 Å)