1QU0

CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN

Summary for 1QU0

• Entry DOI: 10.2210/pdb1qu0/pdb
• Descriptor: LAMININ ALPHA2 CHAIN, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: beta sandwich, calcium-binding protein, metal binding protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Secreted, extracellular space, extracellular matrix, basement membrane: Q60675
• Total number of polymer chains: 4
• Total formula weight: 82513.75

Authors

Hohenester, E.,Tisi, D.,Talts, J.F.,Timpl, R. (deposition date: 1999-07-05, release date: 1999-12-03, Last modification date: 2011-07-13)

Primary citation

Hohenester, E.,Tisi, D.,Talts, J.F.,Timpl, R.
The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin.
Mol.Cell, 4:783-792, 1999

PubMed Abstract: Laminin G-like (LG) modules in the extracellular matrix glycoproteins laminin, perlecan, and agrin mediate the binding to heparin and the cell surface receptor alpha-dystroglycan (alpha-DG). These interactions are crucial to basement membrane assembly, as well as muscle and nerve cell function. The crystal structure of the laminin alpha 2 chain LG5 module reveals a 14-stranded beta sandwich. A calcium ion is bound to one edge of the sandwich by conserved acidic residues and is surrounded by residues implicated in heparin and alpha-DG binding. A calcium-coordinated sulfate ion is suggested to mimic the binding of anionic oligosaccharides. The structure demonstrates a conserved function of the LG module in calcium-dependent lectin-like alpha-DG binding.

PubMed: 10619025
DOI: 10.1016/S1097-2765(00)80388-3

Experimental method

X-RAY DIFFRACTION (2.35 Å)