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1rgi
From Proteopedia
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[[Image:1rgi.gif|left|200px]] | [[Image:1rgi.gif|left|200px]] | ||
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'''Crystal structure of gelsolin domains G1-G3 bound to actin''' | '''Crystal structure of gelsolin domains G1-G3 bound to actin''' | ||
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[[Category: Robinson, R C.]] | [[Category: Robinson, R C.]] | ||
[[Category: Urosev, D.]] | [[Category: Urosev, D.]] | ||
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Revision as of 04:28, 3 May 2008
Crystal structure of gelsolin domains G1-G3 bound to actin
Overview
The actin filament-severing functionality of gelsolin resides in its N-terminal three domains (G1-G3). We have determined the structure of this fragment in complex with an actin monomer. The structure reveals the dramatic domain rearrangements that activate G1-G3, which include the replacement of interdomain interactions observed in the inactive, calcium-free protein by new contacts to actin, and by a novel G2-G3 interface. Together, these conformational changes are critical for actin filament severing, and we suggest that their absence leads to the disease Finnish-type familial amyloidosis. Furthermore, we propose that association with actin drives the calcium-independent activation of isolated G1-G3 during apoptosis, and that a similar mechanism operates to activate native gelsolin at micromolar levels of calcium. This is the first structure of a filament-binding protein bound to actin and it sets stringent, high-resolution limitations on the arrangement of actin protomers within the filament.
About this Structure
1RGI is a Protein complex structure of sequences from Equus caballus and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF., Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC, EMBO J. 2004 Jul 21;23(14):2713-22. Epub 2004 Jun 24. PMID:15215896 Page seeded by OCA on Sat May 3 07:28:10 2008
