2mhu
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The three-dimensional structure of human [113Cd7]metallothionein-2 was | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Braun, W.]] | [[Category: Braun, W.]] | ||
| - | [[Category: Kaegi, J | + | [[Category: Kaegi, J H.R.]] |
| - | [[Category: Messerle, B | + | [[Category: Messerle, B A.]] |
[[Category: Schaeffer, A.]] | [[Category: Schaeffer, A.]] | ||
[[Category: Vasak, M.]] | [[Category: Vasak, M.]] | ||
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[[Category: metallothionein]] | [[Category: metallothionein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:42 2008'' |
Revision as of 16:07, 21 February 2008
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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 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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