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| | {{STRUCTURE_1ji9| PDB=1ji9 | SCENE= }} | | {{STRUCTURE_1ji9| PDB=1ji9 | SCENE= }} |
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| - | '''Solution structure of the alpha-domain of mouse metallothionein-3'''
| + | ===Solution structure of the alpha-domain of mouse metallothionein-3=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11560491}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11560491 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11560491}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 1JI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JI9 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Half turn]] | | [[Category: Half turn]] |
| | [[Category: Type ii turn]] | | [[Category: Type ii turn]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:15:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:17:15 2008'' |
Revision as of 17:17, 1 July 2008
Template:STRUCTURE 1ji9
Solution structure of the alpha-domain of mouse metallothionein-3
Template:ABSTRACT PUBMED 11560491
About this Structure
1JI9 is a Single protein structure of sequence from Mus musculus. Full experimental 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 Tue Jul 1 20:17:15 2008
