1dft
From Proteopedia
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| - | [[Image:1dft.jpg|left|200px]] | + | [[Image:1dft.jpg|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF THE BETA-DOMAIN OF MOUSE METALLOTHIONEIN-1''' | + | {{Structure |
| + | |PDB= 1dft |SIZE=350|CAPTION= <scene name='initialview01'>1dft</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF THE BETA-DOMAIN OF MOUSE METALLOTHIONEIN-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DFT is a [ | + | 1DFT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFT OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy., Zangger K, Oz G, Otvos JD, Armitage IM, Protein Sci. 1999 Dec;8(12):2630-8. PMID:[http:// | + | Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy., Zangger K, Oz G, Otvos JD, Armitage IM, Protein Sci. 1999 Dec;8(12):2630-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10631978 10631978] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: half turn]] | [[Category: half turn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:53 2008'' |
Revision as of 08:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE BETA-DOMAIN OF MOUSE METALLOTHIONEIN-1
Overview
Sequential 1H-NMR assignments of mouse [Cd7]-metallothionein-1 (MT1) have been carried out by standard homonuclear NMR methods and the use of an accordion-heteronuclear multiple quantum correlation (HMQC) experiment for establishing the metal, 113Cd2+, to cysteine connectivities. The three-dimensional structure was then calculated using the distance constraints from two-dimensional nuclear Overhauser effect (NOE) spectroscopy spectra and the Cys-Cd connectivities as input for a distance geometry-dynamical simulated annealing protocol in X-PLOR 3.851. Similar to the mammalian MT2 isoforms, the homologous primary structure of MT1 suggested two separate domains, each containing one metal cluster. Because there were no interdomain constraints, the structure calculation for the N-terminal beta- and the C-terminal alpha-domain were carried out separately. The structures are based on 409 NMR constraints, consisting of 381 NOEs and 28 cysteine-metal connectivities. The only elements of regular secondary structure found were two short stretches of 3(10) helices along with some half-turns in the alpha-domain. Structural comparison with rat liver MT2 showed high similarity, with the beta-domain structure in mouse MT1 showing evidence of increased flexibility compared to the same domain in MT2. The latter was reflected by the presence of fewer interresidue NOEs, no slowly exchanging backbone amide protons, and enhanced cadmium-cadmium exchange rates found in the beta-domain of MT1.
About this Structure
1DFT is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy., Zangger K, Oz G, Otvos JD, Armitage IM, Protein Sci. 1999 Dec;8(12):2630-8. PMID:10631978
Page seeded by OCA on Thu Mar 20 10:37:53 2008
Categories: Mus musculus | Single protein | Armitage, I M. | Otvos, J D. | Oz, G. | Zangger, K. | CD | Cd-s cluster | Half turn
