1spd: Difference between revisions

Revision as of 23:36, 28 July 2008

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File:1spd.png

Template:STRUCTURE 1spd

AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASEAMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE

Template:ABSTRACT PUBMED 8351519

About this StructureAbout this Structure

1SPD is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase., Deng HX, Hentati A, Tainer JA, Iqbal Z, Cayabyab A, Hung WY, Getzoff ED, Hu P, Herzfeldt B, Roos RP, et al., Science. 1993 Aug 20;261(5124):1047-51. PMID:8351519

Page seeded by OCA on Mon Jul 28 23:36:42 2008

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OCA

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-'''AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE'''
+===AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE===
-==Overview==
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-Single-site mutants in the Cu,Zn superoxide dismutase (SOD) gene (SOD1) occur in patients with the fatal neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). Complete screening of the SOD1 coding region revealed that the mutation Ala4 to Val in exon 1 was the most frequent one; mutations were identified in exons 2, 4, and 5 but not in the active site region formed by exon 3. The 2.4 A crystal structure of human SOD, along with two other SOD structures, established that all 12 observed FALS mutant sites alter conserved interactions critical to the beta-barrel fold and dimer contact, rather than catalysis. Red cells from heterozygotes had less than 50 percent normal SOD activity, consistent with a structurally defective SOD dimer. Thus, defective SOD is linked to motor neuron death and carries implications for understanding and possible treatment of FALS.
+The line below this paragraph, {{ABSTRACT_PUBMED_8351519}}, adds the Publication Abstract to the page
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 [[Category: Parge, H E.]]
 [[Category: Tainer, J A.]]
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