1lit
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(New page: 200px<br /> <applet load="1lit" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lit, resolution 1.55Å" /> '''HUMAN LITHOSTATHINE...)
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Revision as of 15:55, 12 November 2007
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HUMAN LITHOSTATHINE
Overview
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.
About this Structure
1LIT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation., Bertrand JA, Pignol D, Bernard JP, Verdier JM, Dagorn JC, Fontecilla-Camps JC, EMBO J. 1996 Jun 3;15(11):2678-84. PMID:8654365
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