1lit

<table><tr><td colspan='2'>[[1lit]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LIT FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lit OCA], [http://pdbe.org/1lit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lit RCSB], [http://www.ebi.ac.uk/pdbsum/1lit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lit ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/REG1A_HUMAN REG1A_HUMAN]] Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8654365</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bernard, J P]]

[[Category: Bertrand, J A]]

[[Category: Dagorn, J C]]

[[Category: Fontacilla-Camps, J C]]

[[Category: Pignol, D]]

[[Category: Verdier, J M]]

[[Category: Pancreatic stone inhibitor]]