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==Crystal structure of CapZ bound to the uncapping motif from CD2AP== | |||
<StructureSection load='3lk4' size='340' side='right' caption='[[3lk4]], [[Resolution|resolution]] 1.99Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3lk4]] is a 36 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. 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> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lk2|3lk2]], [[3lk3|3lk3]]</td></tr> | |||
==Disease== | <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 Gallus gallus]), CAPZA1, CAPZB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 Gallus gallus])</td></tr> | ||
[[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> | <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://www.rcsb.org/pdb/explore.do?structureId=3lk4 RCSB], [http://www.ebi.ac.uk/pdbsum/3lk4 PDBsum]</span></td></tr> | ||
</table> | |||
==Function== | == Disease == | ||
[[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. | [[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. | ||
[[ | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lk/3lk4_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | ==See Also== | ||
*[[CD2-associated protein|CD2-associated protein]] | |||
*[[F-actin capping protein|F-actin capping protein]] | *[[F-actin capping protein|F-actin capping protein]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Cooper, J A | [[Category: Cooper, J A]] | ||
[[Category: Hernandez-Valladares, M | [[Category: Hernandez-Valladares, M]] | ||
[[Category: Kannan, B | [[Category: Kannan, B]] | ||
[[Category: Kim, T | [[Category: Kim, T]] | ||
[[Category: Robinson, R C | [[Category: Robinson, R C]] | ||
[[Category: Tung, A | [[Category: Tung, A]] | ||
[[Category: Actin capping]] | [[Category: Actin capping]] | ||
[[Category: Actin filament]] | [[Category: Actin filament]] | ||
Revision as of 18:42, 18 December 2014
Crystal structure of CapZ bound to the uncapping motif from CD2APCrystal structure of CapZ bound to the uncapping motif from CD2AP
Structural highlights
Disease[CD2AP_HUMAN] Defects in CD2AP are the cause of susceptibility to focal segmental glomerulosclerosis type 3 (FSGS3) [MIM: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.[1] 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. [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.[2] [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. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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