1hl5: Difference between revisions
New page: left|200px<br /> <applet load="1hl5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hl5, resolution 1.80Å" /> '''THE STRUCTURE OF HO... |
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==About this Structure== | ==About this Structure== | ||
1HL5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CU, ZN and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL5 OCA]]. | 1HL5 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CU, ZN and CA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HL5 OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Superoxide dismutase]] | |||
[[Category: Antonyuk, S.]] | [[Category: Antonyuk, S.]] | ||
[[Category: Doucette, P.]] | [[Category: Doucette, P.]] | ||
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[[Category: zn superoxide dismutase]] | [[Category: zn superoxide dismutase]] | ||
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Revision as of 15:24, 30 October 2007
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THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE
OverviewOverview
Cu, Zn superoxide dismutase (SOD1) forms a crucial component of the, cellular defence against oxidative stress. Zn-deficient wild-type and, mutant human SOD1 have been implicated in the disease familial amyotrophic, lateral sclerosis (FALS). We present here the crystal structures of holo, and metal-deficient (apo) wild-type protein at 1.8A resolution. The P21, wild-type holo enzyme structure has nine independently refined dimers and, these combine to form a "trimer of dimers" packing motif in each, asymmetric unit. There is no significant asymmetry between the monomers in, these dimers, in contrast to the subunit structures of the FALS G37R, mutant of human SOD1 and in bovine Cu,Zn SOD. Metal-deficient apo SOD1, crystallizes with two dimers in the asymmetric unit and shows changes in, the ... [(full description)]
About this StructureAbout this Structure
1HL5 is a [Single protein] structure of sequence from [Homo sapiens] with CU, ZN and CA as [ligands]. Active as [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis., Strange RW, Antonyuk S, Hough MA, Doucette PA, Rodriguez JA, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS, J Mol Biol. 2003 May 9;328(4):877-91. PMID:12729761
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OCA- Pages with broken file links
- Homo sapiens
- Single protein
- Superoxide dismutase
- Antonyuk, S.
- Doucette, P.
- Hart, P.J.
- Hasnain, S.S.
- Hayward, L.J.
- Hough, M.A.
- Rodriguez, J.
- Strange, R.W.
- Valentine, J.S.
- CA
- CU
- ZN
- Acetylation
- Amyotrophic lateral sclerosis
- Antioxidant
- Copper
- Disease mutation
- Human cu
- Metal-binding
- Oxidoreductase
- Zinc
- Zn superoxide dismutase