1MHU

THE THREE-DIMENSIONAL STRUCTURE OF HUMAN [113CD7] METALLOTHIONEIN-2 IN SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY

Summary for 1MHU

• Entry DOI: 10.2210/pdb1mhu/pdb
• Descriptor: CD7 METALLOTHIONEIN-2, CADMIUM ION (2 entities in total)
• Functional Keywords: metallothionein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 3475.35

Authors

Braun, W.,Messerle, B.A.,Schaeffer, A.,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 citation

Messerle, B.A.,Schaffer, A.,Vasak, M.,Kagi, J.H.,Wuthrich, K.
Three-dimensional structure of human [113Cd7]metallothionein-2 in solution determined by nuclear magnetic resonance spectroscopy.
J.Mol.Biol., 214:765-779, 1990

PubMed Abstract: 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.

PubMed: 2388267
DOI: 10.1016/0022-2836(90)90291-S

Experimental method

SOLUTION NMR