5wfn

From Proteopedia

(Difference between revisions)

Revision as of 14:44, 6 November 2017

Revised model of leiomodin 2-mediated actin regulation (alternate refinement of PDB 4RWT)

Structural highlights

5wfn is a 4 chain structure with sequence from Drome and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	4rwt
Gene:	Act5C, CG4027 (DROME), LMOD2 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACT1_DROME] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction. [LMOD2_HUMAN] Increases the rate of actin polymerization (PubMed:25250574).^[1]

Publication Abstract from PubMed

Leiomodin (Lmod) is a class of potent tandem-G-actin-binding nucleators in muscle cells. Lmod mutations, deletion, or instability are linked to lethal nemaline myopathy. However, the lack of high-resolution structures of Lmod nucleators in action severely hampered our understanding of their essential cellular functions. Here we report the crystal structure of the actin-Lmod2162-495 nucleus. The structure contains two actin subunits connected by one Lmod2162-495 molecule in a non-filament-like conformation. Complementary functional studies suggest that the binding of Lmod2 stimulates ATP hydrolysis and accelerates actin nucleation and polymerization. The high level of conservation among Lmod proteins in sequence and functions suggests that the mechanistic insights of human Lmod2 uncovered here may aid in a molecular understanding of other Lmod proteins. Furthermore, our structural and mechanistic studies unraveled a previously unrecognized level of regulation in mammalian signal transduction mediated by certain tandem-G-actin-binding nucleators.

Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells.,Chen X, Ni F, Kondrashkina E, Ma J, Wang Q Proc Natl Acad Sci U S A. 2015 Oct 13;112(41):12687-92. doi:, 10.1073/pnas.1512464112. Epub 2015 Sep 28. PMID:26417072^[2]

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

References

↑ Yuen M, Sandaradura SA, Dowling JJ, Kostyukova AS, Moroz N, Quinlan KG, Lehtokari VL, Ravenscroft G, Todd EJ, Ceyhan-Birsoy O, Gokhin DS, Maluenda J, Lek M, Nolent F, Pappas CT, Novak SM, D'Amico A, Malfatti E, Thomas BP, Gabriel SB, Gupta N, Daly MJ, Ilkovski B, Houweling PJ, Davidson AE, Swanson LC, Brownstein CA, Gupta VA, Medne L, Shannon P, Martin N, Bick DP, Flisberg A, Holmberg E, Van den Bergh P, Lapunzina P, Waddell LB, Sloboda DD, Bertini E, Chitayat D, Telfer WR, Laquerriere A, Gregorio CC, Ottenheijm CA, Bonnemann CG, Pelin K, Beggs AH, Hayashi YK, Romero NB, Laing NG, Nishino I, Wallgren-Pettersson C, Melki J, Fowler VM, MacArthur DG, North KN, Clarke NF. Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy. J Clin Invest. 2014 Nov;124(11):4693-708. doi: 10.1172/JCI75199. Epub 2014 Sep, 24. PMID:25250574 doi:http://dx.doi.org/10.1172/JCI75199
↑ Chen X, Ni F, Kondrashkina E, Ma J, Wang Q. Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells. Proc Natl Acad Sci U S A. 2015 Oct 13;112(41):12687-92. doi:, 10.1073/pnas.1512464112. Epub 2015 Sep 28. PMID:26417072 doi:http://dx.doi.org/10.1073/pnas.1512464112

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/5wfn"

@@ Line 3: / Line 3: @@
 <StructureSection load='5wfn' size='340' side='right' caption='[[5wfn]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5wfn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5wfn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WFN FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rwt|4rwt]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Act5C, CG4027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), LMOD2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5wfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wfn OCA], [http://pdbe.org/5wfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wfn RCSB], [http://www.ebi.ac.uk/pdbsum/5wfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wfn ProSAT]</span></td></tr>
 </table>
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Drome]]
+[[Category: Human]]
 [[Category: Dominguez, R]]
 [[Category: Eck, M J]]

5wfn

From Proteopedia

Revision as of 14:44, 6 November 2017

Revised model of leiomodin 2-mediated actin regulation (alternate refinement of PDB 4RWT)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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