1ak7: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
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|RELATEDENTRY=[[1ak6|1AK6]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ak7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ak7 OCA], [http://www.ebi.ac.uk/pdbsum/1ak7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ak7 RCSB]</span> | |||
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[[Category: actin depolymerization factor]] | [[Category: actin depolymerization factor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:01 2008'' | ||
Revision as of 18:42, 30 March 2008
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| Related: | 1AK6
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DESTRIN, NMR, 20 STRUCTURES
OverviewOverview
Destrin is an isoprotein of cofilin that regulates actin cytoskeleton in various eukaryotes. We determined the tertiary structure of destrin by triple-resonance multidimensional nuclear magnetic resonance. In spite of there being no significant amino acid sequence homology, we found that the folding of destrin was strikingly similar to that of repeated segments in the gelsolin family, which resulted in a new protein fold group. Sequential dissimilarity of the actin-binding helix of destrin to that of gelsolin explains the Ca2+-independent actin-binding of destrin. Possible mechanisms of phosphorylation-sensitive phosphoinositide-competitive actin binding, of pH-dependent filament severing, and of nuclear translocation with actin in response to stresses, are discussed on the basis of the tertiary structure.
About this StructureAbout this Structure
1AK7 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
Tertiary structure of destrin and structural similarity between two actin-regulating protein families., Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F, Cell. 1996 Jun 28;85(7):1047-55. PMID:8674111
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