3lk4: Difference between revisions

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-{{Large structure}}
 ==Crystal structure of CapZ bound to the uncapping motif from CD2AP==
-<StructureSection load='3lk4' size='340' side='right' caption='[[3lk4]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
+<StructureSection load='3lk4' size='340' side='right'caption='[[3lk4]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lk4]] is a 36 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=3LK4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LK4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lk4]] is a 36 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=3LK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LK4 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lk2|3lk2]], [[3lk3|3lk3]]</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]] 1.99&#8491;</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]), CAPZA1, 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=3lk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lk4 OCA], [https://pdbe.org/3lk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lk4 RCSB], [https://www.ebi.ac.uk/pdbsum/3lk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lk4 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=3lk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lk4 OCA], [http://pdbe.org/3lk4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lk4 RCSB], [http://www.ebi.ac.uk/pdbsum/3lk4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lk4 ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
-== Disease ==
-[[http://www.uniprot.org/uniprot/CD2AP_HUMAN CD2AP_HUMAN]] Defects in CD2AP are the cause of susceptibility to focal segmental glomerulosclerosis type 3 (FSGS3) [MIM:[http://omim.org/entry/607832 607832]]. A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and edema. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.<ref>PMID:12764198</ref>
 == 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/CD2AP_HUMAN CD2AP_HUMAN]] Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton. May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell. May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis.<ref>PMID:15800069</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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 19: @@
 </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lk4 ConSurf].
 <div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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<ref>PMID:20357771</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3lk4" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[CD2-associated protein|CD2-associated protein]]
+*[[CD2-associated protein 3D structures|CD2-associated protein 3D structures]]
 *[[F-actin capping protein|F-actin capping protein]]
 == References ==
@@ Line 31: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
-[[Category: Cooper, J A]]
+[[Category: Homo sapiens]]
-[[Category: Hernandez-Valladares, M]]
+[[Category: Large Structures]]
-[[Category: Kannan, B]]
+[[Category: Cooper JA]]
-[[Category: Kim, T]]
+[[Category: Hernandez-Valladares M]]
-[[Category: Robinson, R C]]
+[[Category: Kannan B]]
-[[Category: Tung, A]]
+[[Category: Kim T]]
-[[Category: Actin capping]]
+[[Category: Robinson RC]]
-[[Category: Actin filament]]
+[[Category: Tung A]]
-[[Category: Actin-binding]]
-[[Category: Actin-filament regulator]]
-[[Category: Capz]]
-[[Category: Cd2ap]]
-[[Category: Cytoplasm]]
-[[Category: Cytoskeleton]]
-[[Category: Protein binding]]
-[[Category: Protein-protein comple]]
-[[Category: Uncapping]]