3aae
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aae OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aae RCSB], [http://www.ebi.ac.uk/pdbsum/3aae PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aae OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3aae RCSB], [http://www.ebi.ac.uk/pdbsum/3aae PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CAZA1_CHICK CAZA1_CHICK]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line. [[http://www.uniprot.org/uniprot/LR16A_MOUSE LR16A_MOUSE]] Binds CAPZA2 with high affinity and significantly decreases CAPZA2 affinity for actin barbed ends. Increases the rate of elongation from seeds in the presence of CAPZA2, however, seems unable to nucleate filaments. Rapidly uncaps barbed ends capped by CAPZA2 and enhances barbed-end actin polymerization.<ref>PMID:16054028</ref> [[http://www.uniprot.org/uniprot/CAPZB_CHICK CAPZB_CHICK]] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. May play a role in the regulation of cell morphology and cytoskeletal organization. | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Actinin|Actinin]] | ||
+ | *[[F-actin capping protein|F-actin capping protein]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
- | [[Category: Kitazawa, M | + | [[Category: Kitazawa, M]] |
- | [[Category: Maeda, Y | + | [[Category: Maeda, Y]] |
- | [[Category: Minakata, S | + | [[Category: Minakata, S]] |
- | [[Category: Narita, A | + | [[Category: Narita, A]] |
- | [[Category: Nitanai, Y | + | [[Category: Nitanai, Y]] |
- | [[Category: Takeda, S | + | [[Category: Takeda, S]] |
- | [[Category: Yamakuni, T | + | [[Category: Yamakuni, T]] |
[[Category: Actin capping]] | [[Category: Actin capping]] | ||
[[Category: Actin capping protein]] | [[Category: Actin capping protein]] |
Revision as of 20:08, 25 December 2014
Crystal structure of Actin capping protein in complex with CARMIL fragment
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Categories: Gallus gallus | Mus musculus | Kitazawa, M | Maeda, Y | Minakata, S | Narita, A | Nitanai, Y | Takeda, S | Yamakuni, T | Actin capping | Actin capping protein | Actin-binding | Barbed end regulation | Carmil family protein | Cell motility | Conformational change | Cytoskeleton | Isopeptide bond | Leucine-rich repeat | Protein binding