Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity.
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.
Swaminathan
G J
GJ
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom.
Weaver
A J
AJ
Loegering
D A
DA
Checkel
J L
JL
Leonidas
D D
DD
Gleich
G J
GJ
Acharya
K R
KR
D001798:Blood Proteins / Q000737:chemistry*; D003460:Crystallization; D047091:Eosinophil Granule Proteins; D004804:Eosinophils / Q000737:chemistry*; D006801:Humans; D037102:Lectins; D011487:Protein Conformation; D012260:Ribonucleases
D001798:Blood Proteins; D047091:Eosinophil Granule Proteins; D037102:Lectins; D012260:Ribonucleases