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Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.
Author(s) -
Bertrand J. A.,
Pignol D.,
Bernard J. P.,
Verdier J. M.,
Dagorn J. C.,
FontecillaCamps J. C.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb00628.x
Subject(s) - humanities , physics , biology , philosophy
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.

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