1LCL

CHARCOT-LEYDEN CRYSTAL PROTEIN

Summary for 1LCL

• Entry DOI: 10.2210/pdb1lcl/pdb
• Descriptor: LYSOPHOSPHOLIPASE (2 entities in total)
• Functional Keywords: charcot-leyden crystal protein, serine esterase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasmic granule: Q05315
• Total number of polymer chains: 1
• Total formula weight: 16499.89

Authors

Acharya, K.R.,Leonidas, D.D. (deposition date: 1996-01-18, release date: 1997-01-11, Last modification date: 2024-02-14)

Primary citation

Leonidas, D.D.,Elbert, B.L.,Zhou, Z.,Leffler, H.,Ackerman, S.J.,Acharya, K.R.
Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.
Structure, 3:1379-1393, 1995

PubMed Abstract: The Charcot-Leyden crystal (CLC) protein is a major autocrystallizing constituent of human eosinophils and basophils, comprising approximately 10% of the total cellular protein in these granulocytes. Identification of the distinctive hexagonal bipyramidal crystals of CLC protein in body fluids and secretions has long been considered a hallmark of eosinophil-associated allergic inflammation. Although CLC protein possesses lysophospholipase activity, its role(s) in eosinophil or basophil function or associated inflammatory responses has remained speculative.

PubMed: 8747464
DOI: 10.1016/S0969-2126(01)00275-1

Experimental method

X-RAY DIFFRACTION (1.8 Å)