1hl5: Difference between revisions

Revision as of 08:20, 1 July 2008

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File:1hl5.png

Template:STRUCTURE 1hl5

THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASETHE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE

Template:ABSTRACT PUBMED 12729761

About this StructureAbout this Structure

1HL5 is a Single protein structure of sequence from Homo sapiens. 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

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-'''THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE'''
+===THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE===
-==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 metal-binding sites and disorder in the Zn binding and electrostatic loops of one dimer, which is devoid of metals. The second dimer lacks Cu but has approximately 20% occupancy of the Zn site and remains structurally similar to wild-type SOD1. The apo protein forms a continuous, extended arrangement of beta-barrels stacked up along the short crystallographic b-axis, while perpendicular to this axis, the constituent beta-strands form a zig-zag array of filaments, the overall arrangement of which has a similarity to the common structure associated with amyloid-like fibrils.
+The line below this paragraph, {{ABSTRACT_PUBMED_12729761}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12729761 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12729761}}
 ==About this Structure==
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 [[Category: Zinc]]
 [[Category: Zn superoxide dismutase]]
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