2ff3: Difference between revisions
New page: left|200px<br /> <applet load="2ff3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ff3, resolution 2.00Å" /> '''Crystal structure o... |
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[[Image:2ff3.gif|left|200px]]<br /> | [[Image:2ff3.gif|left|200px]]<br /><applet load="2ff3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="2ff3, resolution 2.00Å" /> | caption="2ff3, resolution 2.00Å" /> | ||
'''Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin'''<br /> | '''Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin'''<br /> | ||
==Overview== | ==Overview== | ||
Participation of actin in cellular processes relies on the dynamics of | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2FF3 is a [http://en.wikipedia.org/wiki/Protein_complex 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] with CA and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 2FF3 is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FF3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Aguda, A | [[Category: Aguda, A H.]] | ||
[[Category: Robinson, R | [[Category: Robinson, R C.]] | ||
[[Category: Xue, B.]] | [[Category: Xue, B.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:45 2008'' | ||
Revision as of 18:20, 21 February 2008
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Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Amyloidosis, Finnish type OMIM:[137350]
About this StructureAbout this Structure
2FF3 is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
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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