Sandbox UC 10

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<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png|200px|left|thumb|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>
<StructureSection load='1dq8' size='500' side='right' caption='N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry [[1dxx]])' scene=''>[[Image:1dxx.png|200px|left|thumb|Crystal Structure of Human dystrophin, [[1dxx]]]]Dystrophin is an essential component of skeletal muscle cells. Its N-terminal domain binds to F-actin and its C terminus binds to the dystrophin-associated glycoprotein (DAG) complex in the membrane.<scene name='1xjo/Active_site/3'>active site</scene>
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[[Image:1dxx.png|200px|center|thumb|Crystal Structure of Human dystrophin, [[1dxx]]]]
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CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>[[Image:imag1gonzalo.jpg|right|200px|thumb|Comparacion de la degeneracion muscular, [[1dxx]]]]
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[[Image:imag1gonzalo.jpg|left|200px|thumb|Comparacion de la degeneracion muscular, [[1dxx]]]]
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[[Image:MW_Folding_Simulations.gif|200px|thumb|[[1dxx]]]]
[[Image:MW_Folding_Simulations.gif|200px|thumb|[[1dxx]]]]
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CONCLUSIONS: The dystrophin ABD structure reveals a previously uncharacterised arrangement of the CH domains within the ABD. This observation has implications for the mechanism of actin binding by dystrophin and related proteins. Examining the position of three pathogenic missense mutations within the structure suggests that they exert their effects through misfolding of the ABD, rather than through disruption of the binding to F-actin<ref>PMID 10801490</ref>
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Revision as of 20:20, 19 December 2012

N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN

N-TERMINAL ACTIN-BINDING DOMAIN OF HUMAN DYSTROPHIN (PDB entry 1dxx)

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Referencias

Ref1[2] Ref2 [3]

  1. ↑ Norwood FL, Sutherland-Smith AJ, Keep NH, Kendrick-Jones J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Structure. 2000 May 15;8(5):481-91. PMID:10801490
  2. ↑ Nadeau D, Marchand C. Change in the kinetics of sulphacetamide tissue distribution in Walker tumor-bearing rats. Drug Metab Dispos. 1975 Nov-Dec;3(6):565-76. PMID:1234
  3. ↑ Rubinstein MH. A new granulation method for compressed tablets [proceedings]. J Pharm Pharmacol. 1976 Dec;28 Suppl:67P. PMID:12345
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