2af2
From Proteopedia
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{{STRUCTURE_2af2| PDB=2af2 | SCENE= }} | {{STRUCTURE_2af2| PDB=2af2 | SCENE= }} | ||
- | + | ===Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase=== | |
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- | + | The line below this paragraph, {{ABSTRACT_PUBMED_16291742}}, adds the Publication Abstract to the page | |
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==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2AF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full | + | 2AF2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AF2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Structural proteomics in europe]] | [[Category: Structural proteomics in europe]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:02:11 2008'' |
Revision as of 13:02, 29 July 2008
Contents |
Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase
Template:ABSTRACT PUBMED 16291742
Disease
Known disease associated with this structure: Amyotrophic lateral sclerosis, due to SOD1 deficiency OMIM:[147450]
About this Structure
2AF2 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form., Banci L, Bertini I, Cantini F, D'Amelio N, Gaggelli E, J Biol Chem. 2006 Jan 27;281(4):2333-7. Epub 2005 Nov 14. PMID:16291742
Page seeded by OCA on Tue Jul 29 16:02:11 2008
Categories: Homo sapiens | Single protein | Superoxide dismutase | Amelio, N D. | Banci, L. | Bertini, I. | Cantini, F. | Gaggelli, E. | SPINE, Structural Proteomics in Europe. | Copper depleted protein | Disulfide bond reduced | Homodimeric protein | Human superoxide dismutase | Nmr | Solution structure | Spine | Structural genomic | Structural proteomics in europe