4k17

From Proteopedia

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Current revision

Crystal Structure of mouse CARMIL residues 1-668

Structural highlights

4k17 is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.895Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CARL1_MOUSE Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).^[1]

Publication Abstract from PubMed

CARMIL is an approximately 1,370-amino-acid cytoskeletal scaffold that has crucial roles in cell motility and tissue development through interactions with cytoskeletal effectors and regulation of capping protein at the leading edge. However, the mechanism of CARMIL leading edge localization is unknown. Here we show that CARMIL interacts directly with the plasma membrane through its amino-terminal region. The crystal structure of CARMIL1-668 reveals that this region harbours a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain. Lipid binding is mediated by the PH domain, but is further enhanced by a central helical domain. Small-angle X-ray scattering reveals that the helical domain mediates antiparallel dimerization, properly positioning the PH domains for simultaneous membrane interaction. In cells, deletion of the PH domain impairs leading edge localization. The results support a direct membrane-binding mechanism for CARMIL localization at the leading edge, where it regulates cytoskeletal effectors and motility.

CARMIL leading edge localization depends on a non-canonical PH domain and dimerization.,Zwolak A, Yang C, Feeser EA, Michael Ostap E, Svitkina T, Dominguez R Nat Commun. 2013 Sep 27;4:2523. doi: 10.1038/ncomms3523. PMID:24071777^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yang C, Pring M, Wear MA, Huang M, Cooper JA, Svitkina TM, Zigmond SH. Mammalian CARMIL inhibits actin filament capping by capping protein. Dev Cell. 2005 Aug;9(2):209-21. PMID:16054028 doi:http://dx.doi.org/10.1016/j.devcel.2005.06.008
↑ Zwolak A, Yang C, Feeser EA, Michael Ostap E, Svitkina T, Dominguez R. CARMIL leading edge localization depends on a non-canonical PH domain and dimerization. Nat Commun. 2013 Sep 27;4:2523. doi: 10.1038/ncomms3523. PMID:24071777 doi:http://dx.doi.org/10.1038/ncomms3523

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k17"

Categories: Large Structures | Mus musculus | Dominguez R | Zwolak A

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4k17 is ON HOLD  until Paper Publication
+==Crystal Structure of mouse CARMIL residues 1-668==
+<StructureSection load='4k17' size='340' side='right'caption='[[4k17]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4k17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K17 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.895&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABU:GAMMA-AMINO-BUTANOIC+ACID'>ABU</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=OHB:SALICYLAMIDE'>OHB</scene></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=4k17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k17 OCA], [https://pdbe.org/4k17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k17 RCSB], [https://www.ebi.ac.uk/pdbsum/4k17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k17 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CARL1_MOUSE CARL1_MOUSE] Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization, however, seems unable to nucleate filaments (PubMed:16054028). Plays a role in lamellipodial protrusion formations and cell migration (PubMed:16054028).<ref>PMID:16054028</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+CARMIL is an approximately 1,370-amino-acid cytoskeletal scaffold that has crucial roles in cell motility and tissue development through interactions with cytoskeletal effectors and regulation of capping protein at the leading edge. However, the mechanism of CARMIL leading edge localization is unknown. Here we show that CARMIL interacts directly with the plasma membrane through its amino-terminal region. The crystal structure of CARMIL1-668 reveals that this region harbours a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain. Lipid binding is mediated by the PH domain, but is further enhanced by a central helical domain. Small-angle X-ray scattering reveals that the helical domain mediates antiparallel dimerization, properly positioning the PH domains for simultaneous membrane interaction. In cells, deletion of the PH domain impairs leading edge localization. The results support a direct membrane-binding mechanism for CARMIL localization at the leading edge, where it regulates cytoskeletal effectors and motility.
-Authors: Zwolak, A., Dominguez, R.
+CARMIL leading edge localization depends on a non-canonical PH domain and dimerization.,Zwolak A, Yang C, Feeser EA, Michael Ostap E, Svitkina T, Dominguez R Nat Commun. 2013 Sep 27;4:2523. doi: 10.1038/ncomms3523. PMID:24071777<ref>PMID:24071777</ref>
-Description: Crystal Structure of mouse CARMIL residues 1-668
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4k17" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Dominguez R]]
+[[Category: Zwolak A]]

4k17

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Current revision

Crystal Structure of mouse CARMIL residues 1-668

Structural highlights

Function

Publication Abstract from PubMed

References

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