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1MRT

CONFORMATION OF CD-7 METALLOTHIONEIN-2 FROM RAT LIVER IN AQUEOUS SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Summary for 1MRT
Entry DOI10.2210/pdb1mrt/pdb
DescriptorCD7 METALLOTHIONEIN-2, CADMIUM ION (2 entities in total)
Functional Keywordsmetallothionein
Biological sourceRattus rattus (black rat)
Total number of polymer chains1
Total formula weight3563.41
Authors
Braun, W.,Schultze, P.,Woergoetter, E.,Wagner, G.,Vasak, M.,Kaegi, J.H.R.,Wuthrich, K. (deposition date: 1990-05-14, release date: 1991-04-15, Last modification date: 2024-05-22)
Primary citationSchultze, P.,Worgotter, E.,Braun, W.,Wagner, G.,Vasak, M.,Kagi, J.H.,Wuthrich, K.
Conformation of [Cd7]-metallothionein-2 from rat liver in aqueous solution determined by nuclear magnetic resonance spectroscopy.
J.Mol.Biol., 203:251-268, 1988
Cited by
PubMed Abstract: The three-dimensional structure of [Cd7]-metallothionein-2 from rat liver was determined in aqueous solution, using nuclear magnetic resonance spectrometry and distance geometry calculations. The experimental data provided proton-proton distance constraints from measurements of nuclear Overhauser effects, constraints on the geometry of the metal-cysteine clusters determined by heteronuclear correlation spectroscopy, and dihedral angle constraints derived from both coupling constants and nuclear Overhauser effects. The structure calculations were performed with the program DISMAN. As in previous studies with rabbit liver metallothionein-2a, the structure calculations were performed separately for the alpha and beta-domains containing the 4 and 3-metal clusters, respectively, since no interdomain constraints were found. For both domains, the global polypeptide fold, the location of polypeptide secondary structure elements, the architecture of the metal-sulfur cluster and the local chirality of the metal co-ordination are very similar to the solution structure of rabbit metallothionein-2a, but show considerable difference relative to the crystal structure of rat metallothionein-2.
PubMed: 3184190
DOI: 10.1016/0022-2836(88)90106-4
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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