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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1996-7-30
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1397886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-13990617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1436090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1599470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1644794,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1721241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2185972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2226837,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2332435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2394826,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2463628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2764894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2834230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-2963000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3147713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3290208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3368002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3421951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3665916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-3908481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7509040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7540906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7634089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7704532,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7737575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7760940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-7849594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-8302796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-8438165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8654365-8749859
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2678-84
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:8654365-Amino Acid Sequence,
pubmed-meshheading:8654365-Base Sequence,
pubmed-meshheading:8654365-Calcium-Binding Proteins,
pubmed-meshheading:8654365-Crystallography, X-Ray,
pubmed-meshheading:8654365-Humans,
pubmed-meshheading:8654365-Lithostathine,
pubmed-meshheading:8654365-Models, Molecular,
pubmed-meshheading:8654365-Molecular Sequence Data,
pubmed-meshheading:8654365-Nerve Tissue Proteins,
pubmed-meshheading:8654365-Pancreas,
pubmed-meshheading:8654365-Protein Structure, Tertiary
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pubmed:year |
1996
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pubmed:articleTitle |
Crystal structure of human lithostathine, the pancreatic inhibitor of stone formation.
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pubmed:affiliation |
Laboratoire de Cristallographie et Cristallogénèse des Protéines, Institut de Biologie Structurale J.P. Ebel, CEA-CNRS, France.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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