1spd: Difference between revisions

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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

(as it appears on PubMed at http://www.pubmed.gov), where 8351519 is the PubMed ID number.

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==About this Structure==

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[[Category: Parge, H E.]]

[[Category: Tainer, J A.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 08~~:58:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:36:42 2008''

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-[[Image:1spd.gif|left|200px]]
+{{Seed}}
+[[Image:1spd.png|left|200px]]
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 {{STRUCTURE_1spd|  PDB=1spd  |  SCENE=  }}
-'''AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE'''
+===AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE===
-==Overview==
+<!--
-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
+(as it appears on PubMed at http://www.pubmed.gov), where 8351519 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8351519}}
 ==About this Structure==
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 [[Category: Parge, H E.]]
 [[Category: Tainer, J A.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:58:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:36:42 2008''