1ji9
From Proteopedia
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|PDB= 1ji9 |SIZE=350|CAPTION= <scene name='initialview01'>1ji9</scene> | |PDB= 1ji9 |SIZE=350|CAPTION= <scene name='initialview01'>1ji9</scene> | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ji9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ji9 OCA], [http://www.ebi.ac.uk/pdbsum/1ji9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ji9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Oz, G.]] | [[Category: Oz, G.]] | ||
[[Category: Zangger, K.]] | [[Category: Zangger, K.]] | ||
- | [[Category: CD]] | ||
[[Category: 3-10 helix]] | [[Category: 3-10 helix]] | ||
[[Category: cd-s cluster]] | [[Category: cd-s cluster]] | ||
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[[Category: type ii turn]] | [[Category: type ii turn]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:34:08 2008'' |
Revision as of 18:34, 30 March 2008
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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
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