2ff3
From Proteopedia
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| - | [[Image:2ff3.gif|left|200px]] | + | [[Image:2ff3.gif|left|200px]] |
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| - | '''Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin''' | + | {{Structure |
| + | |PDB= 2ff3 |SIZE=350|CAPTION= <scene name='initialview01'>2ff3</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FF3 is a [ | + | 2FF3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FF3 OCA]. |
==Reference== | ==Reference== | ||
| - | The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins., Aguda AH, Xue B, Irobi E, Preat T, Robinson RC, Structure. 2006 Mar;14(3):469-76. PMID:[http:// | + | The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins., Aguda AH, Xue B, Irobi E, Preat T, Robinson RC, Structure. 2006 Mar;14(3):469-76. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16531231 16531231] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:51:41 2008'' |
Revision as of 14:51, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
Contents |
Overview
Participation of actin in cellular processes relies on the dynamics of filament assembly. Filament elongation is fed by monomeric actin in complex with either profilin or a Wiscott-Aldrich syndrome protein (WASP) homology domain 2 (WH2)/beta-thymosin (betaT) domain. WH2/betaT motif repetition (typified by ciboulot) or combination with nonrelated domains (as found in N-WASP) results in proteins that yield their actin to filament elongation. Here, we report the crystal structures of actin bound hybrid proteins, constructed between gelsolin and WH2/betaT domains from ciboulot or N-WASP. We observe the C-terminal half of ciboulot domain 2 bound to actin. In solution, we show that cibolout domains 2 and 3 bind to both G- and F-actin, and that whole ciboulot forms a complex with two actin monomers. In contrast, the analogous portion of N-WASP WH2 domain 2 is detached from actin, indicating that the C-terminal halves of the betaT and WH2 motifs are not functionally analogous.
Disease
Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]
About this Structure
2FF3 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. Full crystallographic information is available from OCA.
Reference
The structural basis of actin interaction with multiple WH2/beta-thymosin motif-containing proteins., Aguda AH, Xue B, Irobi E, Preat T, Robinson RC, Structure. 2006 Mar;14(3):469-76. PMID:16531231
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