Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.
Identifieur interne : 004298 ( Main/Exploration ); précédent : 004297; suivant : 004299Assembly of synthetic laminin peptides into a triple-stranded coiled-coil structure.
Auteurs : M. Nomizu [États-Unis] ; A. Otaka ; A. Utani ; P P Roller ; Y. YamadaSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1994.
Descripteurs français
- KwdFr :
- Cinétique, Conformation des protéines, Dichroïsme circulaire, Disulfures (métabolisme), Données de séquences moléculaires, Dénaturation des protéines, Fragments peptidiques (), Fragments peptidiques (métabolisme), Fragments peptidiques (synthèse chimique), Laminine (), Laminine (métabolisme), Stabilité de médicament, Structure secondaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Thermodynamique.
- MESH :
- métabolisme : Disulfures, Fragments peptidiques, Laminine.
- synthèse chimique : Fragments peptidiques.
- Cinétique, Conformation des protéines, Dichroïsme circulaire, Données de séquences moléculaires, Dénaturation des protéines, Fragments peptidiques, Laminine, Stabilité de médicament, Structure secondaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Circular Dichroism, Disulfides (metabolism), Drug Stability, Kinetics, Laminin (chemistry), Laminin (metabolism), Macromolecular Substances, Molecular Sequence Data, Peptide Fragments (chemical synthesis), Peptide Fragments (chemistry), Peptide Fragments (metabolism), Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Thermodynamics.
- MESH :
- chemical , chemical synthesis : Peptide Fragments.
- chemical , chemistry : Laminin, Peptide Fragments.
- chemical , metabolism : Disulfides, Laminin, Peptide Fragments.
- Amino Acid Sequence, Circular Dichroism, Drug Stability, Kinetics, Macromolecular Substances, Molecular Sequence Data, Protein Conformation, Protein Denaturation, Protein Structure, Secondary, Thermodynamics.
Abstract
Laminin, a large multidomain glycoprotein specific to basement membranes, is a heterotrimer with alpha, beta, and gamma chains held together in an alpha-helical coiled-coil structure. Synthetic peptides comprising two 51-mers (B1 and B2) from the beta 1 and gamma 1 subunits and a 55-mer (M) from alpha 2 were used to study the molecular mechanisms in laminin chain assembly. Using the synthetic peptides in various mixing experiments, the heterotrimer (B1-B2-M) was preferentially produced. The thermal stability of the heterotrimer increased dramatically (by approximately 20 degrees C) over that of the B1-B2 heterodimer as measured by circular dichroism (CD) spectroscopy. The B1-B1 homodimer (Tm = 60 degrees C) showed higher thermal stability when compared to B1-B2 and B2-B2 dimers. However, the B1 + B2 mixture produced principally the B1-B2 heterodimer. These results suggested that the preferential formations of heterodimer was regulated by kinetic interactions between each chain. The B2 and M peptides have many hydrophobic isoleucine residues which were replaced by leucines. These substitutions were predicted to favor an alpha-helical conformation and a higher propensity for zipper formation. B2L and ML, in which all isoleucine residues were replaced by leucine, showed significantly increased alpha-helicities. While B2L was able to form heterodimers and heterotrimers similar to B2, ML was not able to participate in heterotrimer formation as efficiently as the M peptide. The thermal stability of B1-B2L was comparable to that of B1-B2, but B2L and/or ML containing trimers showed lower thermal stability than B1-B2-M. These results suggest that the isoleucine residues in the alpha 2 and gamma 1 chains are critical for stabilizing the heteromeric triple-stranded coiled-coil structure.
PubMed: 7982952
Affiliations:
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Le document en format XML
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<term>Circular Dichroism</term>
<term>Disulfides (metabolism)</term>
<term>Drug Stability</term>
<term>Kinetics</term>
<term>Laminin (chemistry)</term>
<term>Laminin (metabolism)</term>
<term>Macromolecular Substances</term>
<term>Molecular Sequence Data</term>
<term>Peptide Fragments (chemical synthesis)</term>
<term>Peptide Fragments (chemistry)</term>
<term>Peptide Fragments (metabolism)</term>
<term>Protein Conformation</term>
<term>Protein Denaturation</term>
<term>Protein Structure, Secondary</term>
<term>Thermodynamics</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique</term>
<term>Conformation des protéines</term>
<term>Dichroïsme circulaire</term>
<term>Disulfures (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Fragments peptidiques ()</term>
<term>Fragments peptidiques (métabolisme)</term>
<term>Fragments peptidiques (synthèse chimique)</term>
<term>Laminine ()</term>
<term>Laminine (métabolisme)</term>
<term>Stabilité de médicament</term>
<term>Structure secondaire des protéines</term>
<term>Structures macromoléculaires</term>
<term>Séquence d'acides aminés</term>
<term>Thermodynamique</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptide Fragments</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Laminin</term>
<term>Peptide Fragments</term>
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<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term>
<term>Laminin</term>
<term>Peptide Fragments</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Disulfures</term>
<term>Fragments peptidiques</term>
<term>Laminine</term>
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<term>Circular Dichroism</term>
<term>Drug Stability</term>
<term>Kinetics</term>
<term>Macromolecular Substances</term>
<term>Molecular Sequence Data</term>
<term>Protein Conformation</term>
<term>Protein Denaturation</term>
<term>Protein Structure, Secondary</term>
<term>Thermodynamics</term>
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<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Fragments peptidiques</term>
<term>Laminine</term>
<term>Stabilité de médicament</term>
<term>Structure secondaire des protéines</term>
<term>Structures macromoléculaires</term>
<term>Séquence d'acides aminés</term>
<term>Thermodynamique</term>
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<front><div type="abstract" xml:lang="en">Laminin, a large multidomain glycoprotein specific to basement membranes, is a heterotrimer with alpha, beta, and gamma chains held together in an alpha-helical coiled-coil structure. Synthetic peptides comprising two 51-mers (B1 and B2) from the beta 1 and gamma 1 subunits and a 55-mer (M) from alpha 2 were used to study the molecular mechanisms in laminin chain assembly. Using the synthetic peptides in various mixing experiments, the heterotrimer (B1-B2-M) was preferentially produced. The thermal stability of the heterotrimer increased dramatically (by approximately 20 degrees C) over that of the B1-B2 heterodimer as measured by circular dichroism (CD) spectroscopy. The B1-B1 homodimer (Tm = 60 degrees C) showed higher thermal stability when compared to B1-B2 and B2-B2 dimers. However, the B1 + B2 mixture produced principally the B1-B2 heterodimer. These results suggested that the preferential formations of heterodimer was regulated by kinetic interactions between each chain. The B2 and M peptides have many hydrophobic isoleucine residues which were replaced by leucines. These substitutions were predicted to favor an alpha-helical conformation and a higher propensity for zipper formation. B2L and ML, in which all isoleucine residues were replaced by leucine, showed significantly increased alpha-helicities. While B2L was able to form heterodimers and heterotrimers similar to B2, ML was not able to participate in heterotrimer formation as efficiently as the M peptide. The thermal stability of B1-B2L was comparable to that of B1-B2, but B2L and/or ML containing trimers showed lower thermal stability than B1-B2-M. These results suggest that the isoleucine residues in the alpha 2 and gamma 1 chains are critical for stabilizing the heteromeric triple-stranded coiled-coil structure.</div>
</front>
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