3aae

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:29, 27 September 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3aae' size='340' side='right'caption='[[3aae]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='3aae' size='340' side='right'caption='[[3aae]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3aae]] is a 15 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3aae]] is a 15 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAE 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;'>[[1izn|1izn]], [[3aa0|3aa0]], [[3aa1|3aa1]], [[3aa6|3aa6]], [[3aa7|3aa7]], [[3aaa|3aaa]]</div></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]] 3.3&#8491;</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]), Lrrc16a ([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=3aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aae OCA], [https://pdbe.org/3aae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aae RCSB], [https://www.ebi.ac.uk/pdbsum/3aae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aae 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=3aae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aae OCA], [https://pdbe.org/3aae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aae RCSB], [https://www.ebi.ac.uk/pdbsum/3aae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aae 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/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> [[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.
==See Also==
==See Also==
*[[Actinin 3D structures|Actinin 3D structures]]
*[[Actinin 3D structures|Actinin 3D structures]]
*[[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: 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 protein]]
+
-
[[Category: Actin-binding]]
+
-
[[Category: Barbed end regulation]]
+
-
[[Category: Carmil family protein]]
+
-
[[Category: Cell motility]]
+
-
[[Category: Conformational change]]
+
-
[[Category: Cytoskeleton]]
+
-
[[Category: Isopeptide bond]]
+
-
[[Category: Leucine-rich repeat]]
+
-
[[Category: Protein binding]]
+

Current revision

Crystal structure of Actin capping protein in complex with CARMIL fragment

PDB ID 3aae

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools