Crystallographic determination of lanthanide ion binding to troponin C.
Identifieur interne : 000B46 ( Ncbi/Merge ); précédent : 000B45; suivant : 000B47Crystallographic determination of lanthanide ion binding to troponin C.
Auteurs : O. Herzberg ; M N JamesSource :
- FEBS letters [ 0014-5793 ] ; 1986.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Metals, Rare Earth, Troponin.
- metabolism : Muscles.
- Animals, Binding Sites, Models, Molecular, Protein Binding, Protein Conformation, Troponin C, Turkeys, X-Ray Diffraction.
Abstract
X-ray intensity data to 2.8 A resolution were collected from each of three crystals of turkey skeletal troponin C (TnC) that had been soaked individually in solutions containing the lanthanide ions europium, thulium and lutetium. Each of the resulting difference electron density maps computed for the three data sets showed three lanthanide ion-binding sites on the TnC molecule. Two of the sites are approximately coincident with the Ca2+ positions in binding loops III and IV and the third site is near the Ca2+-free loop I. The mode of ion binding in loop I is different from that commonly observed for Ca2+ in the Ca2+-binding proteins.
PubMed: 3699155
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pubmed:3699155Le document en format XML
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<series><title level="j">FEBS letters</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Binding Sites</term>
<term>Metals, Rare Earth (metabolism)</term>
<term>Models, Molecular</term>
<term>Muscles (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Troponin (metabolism)</term>
<term>Troponin C</term>
<term>Turkeys</term>
<term>X-Ray Diffraction</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Conformation des protéines</term>
<term>Diffraction des rayons X</term>
<term>Dindons</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Muscles (métabolisme)</term>
<term>Sites de fixation</term>
<term>Terres rares (métabolisme)</term>
<term>Troponine (métabolisme)</term>
<term>Troponine C</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Metals, Rare Earth</term>
<term>Troponin</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Muscles</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Muscles</term>
<term>Terres rares</term>
<term>Troponine</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Binding Sites</term>
<term>Models, Molecular</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Troponin C</term>
<term>Turkeys</term>
<term>X-Ray Diffraction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Conformation des protéines</term>
<term>Diffraction des rayons X</term>
<term>Dindons</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Sites de fixation</term>
<term>Troponine C</term>
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<front><div type="abstract" xml:lang="en">X-ray intensity data to 2.8 A resolution were collected from each of three crystals of turkey skeletal troponin C (TnC) that had been soaked individually in solutions containing the lanthanide ions europium, thulium and lutetium. Each of the resulting difference electron density maps computed for the three data sets showed three lanthanide ion-binding sites on the TnC molecule. Two of the sites are approximately coincident with the Ca2+ positions in binding loops III and IV and the third site is near the Ca2+-free loop I. The mode of ion binding in loop I is different from that commonly observed for Ca2+ in the Ca2+-binding proteins.</div>
</front>
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<ArticleTitle>Crystallographic determination of lanthanide ion binding to troponin C.</ArticleTitle>
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<Abstract><AbstractText>X-ray intensity data to 2.8 A resolution were collected from each of three crystals of turkey skeletal troponin C (TnC) that had been soaked individually in solutions containing the lanthanide ions europium, thulium and lutetium. Each of the resulting difference electron density maps computed for the three data sets showed three lanthanide ion-binding sites on the TnC molecule. Two of the sites are approximately coincident with the Ca2+ positions in binding loops III and IV and the third site is near the Ca2+-free loop I. The mode of ion binding in loop I is different from that commonly observed for Ca2+ in the Ca2+-binding proteins.</AbstractText>
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