View source for 1hl5

[[Image:1hl5.gif|left|200px]]<br />
<applet load="1hl5" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1hl5, resolution 1.80&Aring;" />
'''THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE'''<br />

==Overview==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12729761 (full description)]]

==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/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==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12729761 12729761]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Superoxide dismutase]]
[[Category: Antonyuk, S.]]
[[Category: Doucette, P.]]
[[Category: Hart, P.J.]]
[[Category: Hasnain, S.S.]]
[[Category: Hayward, L.J.]]
[[Category: Hough, M.A.]]
[[Category: Rodriguez, J.]]
[[Category: Strange, R.W.]]
[[Category: Valentine, J.S.]]
[[Category: CA]]
[[Category: CU]]
[[Category: ZN]]
[[Category: acetylation]]
[[Category: amyotrophic lateral sclerosis]]
[[Category: antioxidant]]
[[Category: copper]]
[[Category: disease mutation]]
[[Category: human cu]]
[[Category: metal-binding]]
[[Category: oxidoreductase]]
[[Category: zinc]]
[[Category: zn superoxide dismutase]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:38:21 2007''