1LIT

HUMAN LITHOSTATHINE

Summary for 1LIT

• Entry DOI: 10.2210/pdb1lit/pdb
• Descriptor: LITHOSTATHINE (2 entities in total)
• Functional Keywords: pancreatic stone inhibitor, lectin
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P05451
• Total number of polymer chains: 1
• Total formula weight: 16291.04

Authors

Bertrand, J.A.,Pignol, D.,Bernard, J.-P.,Verdier, J.-M.,Dagorn, J.-C.,Fontacilla-Camps, J.C. (deposition date: 1996-01-17, release date: 1997-01-11, Last modification date: 2024-11-20)

Primary citation

Bertrand, J.A.,Pignol, D.,Bernard, J.P.,Verdier, J.M.,Dagorn, J.C.,Fontecilla-Camps, J.C.
Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.
EMBO J., 15:2678-2684, 1996

PubMed Abstract: Human lithostathine (HLIT) is a pancreatic glycoprotein which inhibits the growth and nucleation of calcium carbonate crystals. The crystal structure of the monomeric 17 kDa HLIT, determined to a resolution of 1.55 angstroms, was refined to a crystallographic R-factor of 18.6%. Structural comparison with the carbohydrate-recognition domains of rat mannose-binding protein and E-selectin indicates that the C-terminal domain of HLIT shares a common architecture with the C-type lectins. Nevertheless, HLIT does not bind carbohydrate nor does it contain the characteristic calcium-binding sites of the C-type lectins. In consequence, HLIT represents the first structurally characterized member of this superfamily which is not a lectin. Analysis of the charge distribution and calculation of its dipole moment reveal that HLIT is a strongly polarized molecule. Eight acidic residues which are separated by regular 6 angstrom spacings form a unique and continuous patch on the molecular surface. This arrangement coincides with the distribution of calcium ions on certain planes of the calcium carbonate crystal; the dipole moment of HLIT may play a role in orienting the protein on the crystal surface prior to the more specific interactions of the acidic residues.

PubMed: 8654365

Experimental method

X-RAY DIFFRACTION (1.55 Å)