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==Solution NMR structure of V-1 bound to capping protein (CP)==
==Solution NMR structure of V-1 bound to capping protein (CP)==
<StructureSection load='2kxp' size='340' side='right'caption='[[2kxp]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2kxp' size='340' side='right'caption='[[2kxp]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kxp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kxp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXP FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1myo|1myo]], [[1izn|1izn]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAPZA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), CAPZB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), Mtpn, Gcdp ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2kxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxp OCA], [https://pdbe.org/2kxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxp RCSB], [https://www.ebi.ac.uk/pdbsum/2kxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxp ProSAT]</span></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=2kxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxp OCA], [https://pdbe.org/2kxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxp RCSB], [https://www.ebi.ac.uk/pdbsum/2kxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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. [[https://www.uniprot.org/uniprot/MTPN_MOUSE MTPN_MOUSE]] Promotes dimerization of NF-kappa-B subunits and regulates NF-kappa-B transcription factor activity. Promotes growth of cardiomyocytes, but not cardiomyocyte proliferation. Promotes cardiac muscle hypertrophy (By similarity). Plays a role in the regulation of the growth of actin filaments. Inhibits the activity of the F-actin-capping protein complex formed by the CAPZA1 and CAPZB heterodimer.<ref>PMID:20538588</ref>  [[https://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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==See Also==
==See Also==
*[[F-actin capping protein|F-actin capping protein]]
*[[F-actin capping protein|F-actin capping protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Chick]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Fujiwara, I]]
[[Category: Fujiwara I]]
[[Category: III, J A.Hammer]]
[[Category: Hammer III JA]]
[[Category: Tjandra, N]]
[[Category: Tjandra N]]
[[Category: Zwolak, A]]
[[Category: Zwolak A]]
[[Category: Capping protein]]
[[Category: Protein binding]]
[[Category: Protein-protein interaction]]
[[Category: V-1]]

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