1lit
From Proteopedia
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| - | [[Image:1lit.gif|left|200px]] | + | [[Image:1lit.gif|left|200px]] |
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| - | '''HUMAN LITHOSTATHINE''' | + | {{Structure |
| + | |PDB= 1lit |SIZE=350|CAPTION= <scene name='initialview01'>1lit</scene>, resolution 1.55Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN LITHOSTATHINE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LIT is a [ | + | 1LIT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LIT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8654365 8654365] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: pancreatic stone inhibitor]] | [[Category: pancreatic stone inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:23 2008'' |
Revision as of 10:31, 20 March 2008
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| , resolution 1.55Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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