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1ji9
From Proteopedia
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| - | [[Image:1ji9.jpg|left|200px]] | + | [[Image:1ji9.jpg|left|200px]] |
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| - | '''Solution structure of the alpha-domain of mouse metallothionein-3''' | + | {{Structure |
| + | |PDB= 1ji9 |SIZE=350|CAPTION= <scene name='initialview01'>1ji9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of the alpha-domain of mouse metallothionein-3''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JI9 is a [ | + | 1JI9 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=1JI9 OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3., Oz G, Zangger K, Armitage IM, Biochemistry. 2001 Sep 25;40(38):11433-41. PMID:[http:// | + | Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3., Oz G, Zangger K, Armitage IM, Biochemistry. 2001 Sep 25;40(38):11433-41. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11560491 11560491] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: type ii turn]] | [[Category: type ii 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 12:03:47 2008'' |
Revision as of 10:03, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of the alpha-domain of mouse metallothionein-3
Overview
The brain specific member of the metallothionein (MT) family of proteins, metallothionein-3, inhibits the growth and survival of neurons, in contrast to the ubiquitous mammalian MT isoforms, MT-1 and MT-2, that are found in most tissues and are thought to function in metal ion homeostasis and detoxification. Solution NMR was utilized to determine the structural and dynamic differences of MT-3 from MT-1 and 2. The high-resolution solution structure of the C-terminal alpha-domain of recombinant mouse MT-3 revealed a tertiary fold very similar to MT-1 and 2, except for a loop that accommodates an acidic insertion relative to these isoforms. This loop was distinguished from the rest of the domain by dynamics of the backbone on the nano- to picosecond time-scale shown by (15)N relaxation studies and was identified as a possible interaction site with other proteins. The N-terminal beta-domain contains the region responsible for the growth inhibitory activity, a CPCP tetrapeptide close to the N-terminus. Because of exchange broadening of a large number of the NMR signals from this domain, homology modeling was utilized to calculate models for the beta-domain and suggested that while the backbone fold of the MT-3 beta-domain is identical to MT-1 and 2, the second proline responsible for the activity, Pro9, may show structural heterogeneity. (15)N relaxation analyses implied fast internal motions for the beta-domain. On the basis of these observations, we conclude that the growth inhibitory activity exhibited by MT-3 is a result of a combination of local structural differences and global dynamics in the beta-domain.
About this Structure
1JI9 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: metallothionein-3., Oz G, Zangger K, Armitage IM, Biochemistry. 2001 Sep 25;40(38):11433-41. PMID:11560491
Page seeded by OCA on Thu Mar 20 12:03:47 2008
Categories: Mus musculus | Single protein | Armitage, I M. | Oz, G. | Zangger, K. | CD | 3-10 helix | Cd-s cluster | Half turn | Type ii turn
