2mhu
From Proteopedia
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THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Overview
The three-dimensional structure of human [113Cd7]metallothionein-2 was, determined by nuclear magnetic resonance spectroscopy in solution., Sequence-specific 1H resonance assignments were obtained using the, sequential assignment method. The input for the structure calculations, consisted of the metal-cysteine co-ordinative bonds identified with, heteronuclear correlation spectroscopy, 1H-1H distance constraints from, nuclear Overhauser enhancement spectroscopy, and spin-spin coupling, constants 3JHN alpha and 3J alpha beta. The molecule consists of two, domains, the beta-domain including amino acid residues 1 to 30 and three, metal ions, and the alpha-domain including residues 31 to 61 and four, metal ions. The nuclear magnetic resonance data present no evidence for a, preferred relative orientation of the two domains. The, polypeptide-to-metal co-ordinative bonds in human metallothionein-2 are, identical to those in the previously determined solution structures of rat, metallothionein-2 and rabbit metallothionein-2a, and the polypeptide, conformations in the three proteins are also closely similar.
About this Structure
2MHU is a Single protein structure of sequence from Homo sapiens with CD as ligand. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy., Messerle BA, Schaffer A, Vasak M, Kagi JH, Wuthrich K, J Mol Biol. 1990 Aug 5;214(3):765-79. PMID:2388267
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