Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation. Export

@article{citeulike:2925801, 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.}, address = {Laboratoire de Cristallographie et Cristallog\'{e}n\`{e}se des Prot\'{e}ines, Institut de Biologie Structurale J.P. Ebel, CEA-CNRS, France.}, author = {Bertrand, J. A. and Pignol, D. and Bernard, J. P. and Verdier, J. M. and Dagorn, J. C. and Fontecilla-Camps, J. C.}, citeulike-article-id = {2925801}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/8654365}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=8654365}, day = {3}, issn = {0261-4189}, journal = {The EMBO journal}, keywords = {ithostathine}, month = {June}, number = {11}, pages = {2678--2684}, posted-at = {2008-06-25 13:06:54}, priority = {2}, title = {Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/8654365}, volume = {15}, year = {1996} }

TY - JOUR ID - citeulike:2925801 L3 - citeulike-article-id:2925801 N2 - 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. IS - 11 JF - The EMBO journal SN - 0261-4189 AD - Laboratoire de Cristallographie et Cristallogénèse des Protéines, Institut de Biologie Structurale J.P. Ebel, CEA-CNRS, France. EP - 2684 TI - Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation. VL - 15 SP - 2678 KW - ithostathine AU - Bertrand, JA AU - Pignol, D AU - Bernard, JP AU - Verdier, JM AU - Dagorn, JC AU - Fontecilla-Camps, JC PY - 1996/06/03/ UR - http://view.ncbi.nlm.nih.gov/pubmed/8654365 ER -