1lit: Difference between revisions

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New page: left|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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[[Image:1lit.gif|left|200px]]<br />
<applet load="1lit" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lit, resolution 1.55&Aring;" />
'''HUMAN LITHOSTATHINE'''<br />


==Overview==
==HUMAN LITHOSTATHINE==
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.
<StructureSection load='1lit' size='340' side='right'caption='[[1lit]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lit]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1LIT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lit OCA], [https://pdbe.org/1lit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lit RCSB], [https://www.ebi.ac.uk/pdbsum/1lit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lit ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/li/1lit_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lit ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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>
1LIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LIT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8654365 8654365]
</div>
<div class="pdbe-citations 1lit" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bernard, J.P.]]
[[Category: Bernard J-P]]
[[Category: Bertrand, J.A.]]
[[Category: Bertrand JA]]
[[Category: Dagorn, J.C.]]
[[Category: Dagorn J-C]]
[[Category: Fontacilla-Camps, J.C.]]
[[Category: Fontacilla-Camps JC]]
[[Category: Pignol, D.]]
[[Category: Pignol D]]
[[Category: Verdier, J.M.]]
[[Category: Verdier J-M]]
[[Category: lectin]]
[[Category: pancreatic stone inhibitor]]
 
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Latest revision as of 00:12, 21 November 2024

HUMAN LITHOSTATHINE

1lit, resolution 1.55Å

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