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| | <StructureSection load='3lk2' size='340' side='right'caption='[[3lk2]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='3lk2' size='340' side='right'caption='[[3lk2]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3lk2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LK2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3lk2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LK2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1izn|1izn]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAPZA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), CAPZB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3lk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lk2 OCA], [https://pdbe.org/3lk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lk2 RCSB], [https://www.ebi.ac.uk/pdbsum/3lk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lk2 ProSAT]</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=3lk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lk2 OCA], [http://pdbe.org/3lk2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lk2 RCSB], [http://www.ebi.ac.uk/pdbsum/3lk2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lk2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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_HUMAN LR16A_HUMAN]] 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 (By similarity).<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. | + | [https://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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aguda, A H]] | + | [[Category: Aguda AH]] |
| - | [[Category: Cooper, J A]] | + | [[Category: Cooper JA]] |
| - | [[Category: Hernandez-Valladares, M]] | + | [[Category: Hernandez-Valladares M]] |
| - | [[Category: Kannan, B]] | + | [[Category: Kannan B]] |
| - | [[Category: Kim, T]] | + | [[Category: Kim T]] |
| - | [[Category: Larsson, M]] | + | [[Category: Larsson M]] |
| - | [[Category: Robinson, R C]] | + | [[Category: Robinson RC]] |
| - | [[Category: Tung, A]] | + | [[Category: Tung A]] |
| - | [[Category: Actin capping]]
| + | |
| - | [[Category: Actin filament]]
| + | |
| - | [[Category: Actin-binding]]
| + | |
| - | [[Category: Actin-filament regulator]]
| + | |
| - | [[Category: Capz]]
| + | |
| - | [[Category: Carmil]]
| + | |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein-protein complex]]
| + | |
| - | [[Category: Uncapping]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Capping protein (CP) regulates actin dynamics by binding the barbed ends of actin filaments. Removal of CP may be one means to harness actin polymerization for processes such as cell movement and endocytosis. Here we structurally and biochemically investigated a CP interaction (CPI) motif present in the otherwise unrelated proteins CARMIL and CD2AP. The CPI motif wraps around the stalk of the mushroom-shaped CP at a site distant from the actin-binding interface, which lies on the top of the mushroom cap. We propose that the CPI motif may act as an allosteric modulator, restricting CP to a low-affinity, filament-binding conformation. Structure-based sequence alignments extend the CPI motif-containing family to include CIN85, CKIP-1, CapZIP and a relatively uncharacterized protein, WASHCAP (FAM21). Peptides comprising these CPI motifs are able to inhibit CP and to uncap CP-bound actin filaments.
Structural characterization of a capping protein interaction motif defines a family of actin filament regulators.,Hernandez-Valladares M, Kim T, Kannan B, Tung A, Aguda AH, Larsson M, Cooper JA, Robinson RC Nat Struct Mol Biol. 2010 Apr;17(4):497-503. Epub 2010 Mar 28. PMID:20357771[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hernandez-Valladares M, Kim T, Kannan B, Tung A, Aguda AH, Larsson M, Cooper JA, Robinson RC. Structural characterization of a capping protein interaction motif defines a family of actin filament regulators. Nat Struct Mol Biol. 2010 Apr;17(4):497-503. Epub 2010 Mar 28. PMID:20357771 doi:10.1038/nsmb.1792
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