2yle

From Proteopedia

(Difference between revisions)

Revision as of 09:58, 4 August 2016

Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide

Structural highlights

2yle is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2ylf
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SPIR1_HUMAN] Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis.^[1] ^[2] [FMN2_HUMAN] Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.^[3] ^[4]

Publication Abstract from PubMed

The distinct actin nucleation factors of the Spir and formin subgroup families cooperate in actin nucleation. The Spir/formin cooperativity has been identified to direct two essential steps in mammalian oocyte maturation, the asymmetric spindle positioning and polar body extrusion during meiosis. Understanding the nature and regulation of the Spir/Fmn cooperation is an important requirement to comprehend mammalian reproduction. Recently we dissected the structural elements of the Spir and Fmn family proteins, which physically link the two actin nucleation factors. The trans-regulatory interaction is mediated by the Spir kinase non-catalytic C-lobe domain (KIND) and the C-terminal formin Spir interaction motif (FSI). The interaction inhibits formin nucleation activity and enhances the Spir activity. To get insights into the molecular mechanism of the Spir/Fmn interaction, we determined the crystal structure of the KIND domain alone and in complex with the C-terminal Fmn-2 FSI peptide. Together they confirm the proposed structural homology of the KIND domain to the protein kinase fold and reveal the basis of the Spir/formin interaction. The complex structure showed a large interface with conserved and positively charged residues of the Fmn FSI peptide mediating major contacts to an acidic groove on the surface of KIND. Protein interaction studies verified the electrostatic nature of the interaction. The data presented here provide the molecular basis of the Spir/formin interaction and give a first structural view into the mechanisms of actin nucleation factor cooperativity.

Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex.,Zeth K, Pechlivanis M, Samol A, Pleiser S, Vonrhein C, Kerkhoff E J Biol Chem. 2011 Sep 2;286(35):30732-9. Epub 2011 Jun 26. PMID:21705804^[5]

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

References

↑ Kerkhoff E, Simpson JC, Leberfinger CB, Otto IM, Doerks T, Bork P, Rapp UR, Raabe T, Pepperkok R. The Spir actin organizers are involved in vesicle transport processes. Curr Biol. 2001 Dec 11;11(24):1963-8. PMID:11747823
↑ Pfender S, Kuznetsov V, Pleiser S, Kerkhoff E, Schuh M. Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division. Curr Biol. 2011 Jun 7;21(11):955-60. doi: 10.1016/j.cub.2011.04.029. Epub 2011, May 27. PMID:21620703 doi:http://dx.doi.org/10.1016/j.cub.2011.04.029
↑ Peng KW, Liou YM. Differential role of actin-binding proteins in controlling the adipogenic differentiation of human CD105-positive Wharton's Jelly cells. Biochim Biophys Acta. 2012 Apr;1820(4):469-81. doi: 10.1016/j.bbagen.2012.01.014., Epub 2012 Feb 8. PMID:22330775 doi:http://dx.doi.org/10.1016/j.bbagen.2012.01.014
↑ Yamada K, Ono M, Perkins ND, Rocha S, Lamond AI. Identification and functional characterization of FMN2, a regulator of the cyclin-dependent kinase inhibitor p21. Mol Cell. 2013 Mar 7;49(5):922-33. doi: 10.1016/j.molcel.2012.12.023. Epub 2013, Jan 31. PMID:23375502 doi:http://dx.doi.org/10.1016/j.molcel.2012.12.023
↑ Zeth K, Pechlivanis M, Samol A, Pleiser S, Vonrhein C, Kerkhoff E. Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)*formin-2 formin SPIR interaction motif (FSI) complex. J Biol Chem. 2011 Sep 2;286(35):30732-9. Epub 2011 Jun 26. PMID:21705804 doi:10.1074/jbc.M111.257782

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/2yle"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide==
 <StructureSection load='2yle' size='340' side='right' caption='[[2yle]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2yle]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2yle]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YLE FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ylf|2ylf]]</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=2yle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yle OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yle RCSB], [http://www.ebi.ac.uk/pdbsum/2yle PDBsum]</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=2yle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yle OCA], [http://pdbe.org/2yle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yle RCSB], [http://www.ebi.ac.uk/pdbsum/2yle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yle ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FMN2_HUMAN FMN2_HUMAN]] Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.<ref>PMID:22330775</ref> <ref>PMID:23375502</ref>
+[[http://www.uniprot.org/uniprot/SPIR1_HUMAN SPIR1_HUMAN]] Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis.<ref>PMID:11747823</ref> <ref>PMID:21620703</ref>  [[http://www.uniprot.org/uniprot/FMN2_HUMAN FMN2_HUMAN]] Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation.<ref>PMID:22330775</ref> <ref>PMID:23375502</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2yle" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Homo sapiens]]
+[[Category: Human]]
 [[Category: Kerkhoff, E]]
 [[Category: Pechlivanis, M]]

2yle

From Proteopedia

Revision as of 09:58, 4 August 2016

Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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