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J Biol Chem, Vol. 275, Issue 2, 1057-1064, January 14, 2000
From the Pancreatic juice is supersaturated with calcium
carbonate. Calcite crystals therefore may occur, obstruct pancreatic
ducts, and finally cause a lithiasis. Human lithostathine, a protein synthesized by the pancreas, inhibits the growth of calcite crystals by
inducing a habit modification: the rhombohedral {10 The atomic coordinates and structure factors (code 1QDD) have
been deposited in the Protein Data Bank, Research Collaboratory for
Structural Bioinformatics, Rutgers University, New Brunswick, NJ
(http://www.rcsb.org/).
Mechanism of Calcite Crystal Growth Inhibition by the N-terminal
Undecapeptide of Lithostathine*
,
,,, and
Laboratoire de Génie Chimique,
Unité Mixte de Recherche CNRS 5503, Ecole Nationale
Supérieure de Génie Chimique-Institut National
Polytechnique de Toulouse/Université Paul Sabatier, Toulouse,
Cedex 4 31078, France, the § Laboratoire de Cristallographie
et de Cristallogenèse des Protéines, Institut di Biologie
Structurale Commissariat à l'Energie Atomique-CNRS, Grenoble,
Cedex 1 38027, France, the ¶ Laboratoire d'Ingénierie des
Systèmes Macromoléculaires, Unite Propre di Recherche CNRS
9027, Marseille, 13009 France, the Service de Néphrologie,
Hôpital Sainte-Marguerite, Marseille, 13385 France, and the
** Unité Propre de Recherche et d'Enseignement Supérieur
Associeé CNRS 6032, Faculté de Pharmacie,
13385 Marseille Cedex 05, France
4} usual habit is transformed into a needle-like habit through the {11 
0} crystal form. A similar observation was made with the
N-terminal undecapeptide (pE1R11) of
lithostathine. We therefore aimed at discovering how peptides inhibit
calcium salt crystal growth. We solved the complete x-ray structure of
lithostathine, including the flexible N-terminal domain, at 1.3 Å.
Docking studies of pE1R11 with the (10 4) and (11 0) faces through molecular dynamics simulation
resulted in three successive steps. First, the undecapeptide progressively unfolded as it approached the calcite surface. Second, mobile lateral chains of amino acids made hydrogen bonds with the
calcite surface. Last, electrostatic bonds between calcium ions and
peptide bonds stabilized and anchored pE1R11 on
the crystal surface. pE1R11-calcite interaction
was stronger with the (11 0) face than with the (10 4)
face, confirming earlier experimental observations. Energy
contributions showed that the peptide backbone governed the binding
more than did the lateral chains. The ability of peptides to inhibit
crystal growth is therefore essentially based on backbone flexibility.
*
This work was supported by Grant ACC-SV 5 from the
Ministère de l'Enseignement Supérieur et de la Recherche.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: UPRESA CNRS 6032, Faculté de Pharmacie, 27 Bd. Jean Moulin, 13385 Marseille Cedex 05, France. Tel./Fax: 33-4-91-83-55-07; E-mail: verdier@
pharmacie.univ-mrs.fr.
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