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| - | [[Image:2i0n.gif|left|200px]] | |
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| - | {{Structure
| + | ==Structure of Dictyostelium discoideum Myosin VII SH3 domain with adjacent proline rich region== |
| - | |PDB= 2i0n |SIZE=350|CAPTION= <scene name='initialview01'>2i0n</scene>
| + | <StructureSection load='2i0n' size='340' side='right'caption='[[2i0n]]' scene=''> |
| - | |SITE= | + | == Structural highlights == |
| - | |LIGAND=
| + | <table><tr><td colspan='2'>[[2i0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I0N FirstGlance]. <br> |
| - | |ACTIVITY=
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | |GENE= myoI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum]) | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2i0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i0n OCA], [https://pdbe.org/2i0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i0n RCSB], [https://www.ebi.ac.uk/pdbsum/2i0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i0n ProSAT]</span></td></tr> |
| - | }}
| + | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MYOI_DICDI MYOI_DICDI] Myosins are actin-based motor molecules with ATPase activity. Involved in the early steps of phagocytosis and adhesion.<ref>PMID:10574761</ref> <ref>PMID:11267868</ref> <ref>PMID:15826949</ref> |
| | + | == 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/i0/2i0n_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/main_output.php?pdb_ID=2i0n ConSurf]. |
| | + | <div style="clear:both"></div> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Myosins play essential roles in migration, cytokinesis, endocytosis, and adhesion. They are composed of a large N-terminal motor domain with ATPase and actin binding sites and C-terminal neck and tail regions, whose functional roles and structural context in the protein are less well characterized. The tail regions of myosins I, IV, VII, XII, and XV each contain a putative SH3 domain that may be involved in protein-protein interactions. SH3 domains are reported to bind proline-rich motifs, especially "PxxP" sequences, and such interactions serve regulatory functions. The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Here, we use NMR spectroscopy to reveal the structure of a protein construct from Dictyostelium myosin VII (DdM7) spanning A1620-T1706, which contains its SH3 domain and adjacent proline-rich region. The SH3 domain forms the signature beta-barrel architecture found in other SH3 domains, with conserved tryptophan and tyrosine residues forming a hydrophobic pocket known to bind "PxxP" motifs. In addition, acidic residues in the RT or n-Src loops are available to interact with the basic anchoring residues that are typically found in ligands or proteins that bind SH3 domains. The DdM7 SH3 differs in the hydrophobicity of the second pocket formed by the 3(10) helix and following beta-strand, which contains polar rather than hydrophobic side chains. Most unusual, however, is that this domain binds its adjacent proline-rich region at a surface remote from the region previously identified to bind "PxxP" motifs. The interaction may affect the orientation of the tail without sacrificing the availability of the canonical "PxxP"-binding surface. |
| | | | |
| - | '''Structure of Dictyostelium discoideum Myosin VII SH3 domain with adjacent proline rich region'''
| + | The SH3 domain of a M7 interacts with its C-terminal proline-rich region.,Wang Q, Deloia MA, Kang Y, Litchke C, Zhang N, Titus MA, Walters KJ Protein Sci. 2007 Feb;16(2):189-96. Epub 2006 Dec 22. PMID:17189480<ref>PMID:17189480</ref> |
| | | | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 2i0n" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Overview== | + | ==See Also== |
| - | Myosins play essential roles in migration, cytokinesis, endocytosis, and adhesion. They are composed of a large N-terminal motor domain with ATPase and actin binding sites and C-terminal neck and tail regions, whose functional roles and structural context in the protein are less well characterized. The tail regions of myosins I, IV, VII, XII, and XV each contain a putative SH3 domain that may be involved in protein-protein interactions. SH3 domains are reported to bind proline-rich motifs, especially "PxxP" sequences, and such interactions serve regulatory functions. The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Here, we use NMR spectroscopy to reveal the structure of a protein construct from Dictyostelium myosin VII (DdM7) spanning A1620-T1706, which contains its SH3 domain and adjacent proline-rich region. The SH3 domain forms the signature beta-barrel architecture found in other SH3 domains, with conserved tryptophan and tyrosine residues forming a hydrophobic pocket known to bind "PxxP" motifs. In addition, acidic residues in the RT or n-Src loops are available to interact with the basic anchoring residues that are typically found in ligands or proteins that bind SH3 domains. The DdM7 SH3 differs in the hydrophobicity of the second pocket formed by the 3(10) helix and following beta-strand, which contains polar rather than hydrophobic side chains. Most unusual, however, is that this domain binds its adjacent proline-rich region at a surface remote from the region previously identified to bind "PxxP" motifs. The interaction may affect the orientation of the tail without sacrificing the availability of the canonical "PxxP"-binding surface.
| + | *[[Myosin 3D Structures|Myosin 3D Structures]] |
| - | | + | == References == |
| - | ==About this Structure==
| + | <references/> |
| - | 2I0N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I0N OCA].
| + | __TOC__ |
| - | | + | </StructureSection> |
| - | ==Reference== | + | |
| - | The SH3 domain of a M7 interacts with its C-terminal proline-rich region., Wang Q, Deloia MA, Kang Y, Litchke C, Zhang N, Titus MA, Walters KJ, Protein Sci. 2007 Feb;16(2):189-96. Epub 2006 Dec 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17189480 17189480]
| + | |
| | [[Category: Dictyostelium discoideum]] | | [[Category: Dictyostelium discoideum]] |
| - | [[Category: Single protein]] | + | [[Category: Large Structures]] |
| - | [[Category: Deloia, M A.]] | + | [[Category: Deloia MA]] |
| - | [[Category: Kang, Y.]] | + | [[Category: Kang Y]] |
| - | [[Category: Litchke, C.]] | + | [[Category: Litchke C]] |
| - | [[Category: Titus, M A.]] | + | [[Category: Titus MA]] |
| - | [[Category: Walters, K J.]] | + | [[Category: Walters KJ]] |
| - | [[Category: Wang, Q.]] | + | [[Category: Wang Q]] |
| - | [[Category: beta-sheet loop]]
| + | |
| - | | + | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:23:59 2008''
| + | |
| Structural highlights
Function
MYOI_DICDI Myosins are actin-based motor molecules with ATPase activity. Involved in the early steps of phagocytosis and adhesion.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Myosins play essential roles in migration, cytokinesis, endocytosis, and adhesion. They are composed of a large N-terminal motor domain with ATPase and actin binding sites and C-terminal neck and tail regions, whose functional roles and structural context in the protein are less well characterized. The tail regions of myosins I, IV, VII, XII, and XV each contain a putative SH3 domain that may be involved in protein-protein interactions. SH3 domains are reported to bind proline-rich motifs, especially "PxxP" sequences, and such interactions serve regulatory functions. The activity of Src, PI3, and Itk kinases, for example, is regulated by intramolecular interactions between their SH3 domain and internal proline-rich sequences. Here, we use NMR spectroscopy to reveal the structure of a protein construct from Dictyostelium myosin VII (DdM7) spanning A1620-T1706, which contains its SH3 domain and adjacent proline-rich region. The SH3 domain forms the signature beta-barrel architecture found in other SH3 domains, with conserved tryptophan and tyrosine residues forming a hydrophobic pocket known to bind "PxxP" motifs. In addition, acidic residues in the RT or n-Src loops are available to interact with the basic anchoring residues that are typically found in ligands or proteins that bind SH3 domains. The DdM7 SH3 differs in the hydrophobicity of the second pocket formed by the 3(10) helix and following beta-strand, which contains polar rather than hydrophobic side chains. Most unusual, however, is that this domain binds its adjacent proline-rich region at a surface remote from the region previously identified to bind "PxxP" motifs. The interaction may affect the orientation of the tail without sacrificing the availability of the canonical "PxxP"-binding surface.
The SH3 domain of a M7 interacts with its C-terminal proline-rich region.,Wang Q, Deloia MA, Kang Y, Litchke C, Zhang N, Titus MA, Walters KJ Protein Sci. 2007 Feb;16(2):189-96. Epub 2006 Dec 22. PMID:17189480[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Titus MA. A class VII unconventional myosin is required for phagocytosis. Curr Biol. 1999 Nov 18;9(22):1297-303. PMID:10574761
- ↑ Tuxworth RI, Weber I, Wessels D, Addicks GC, Soll DR, Gerisch G, Titus MA. A role for myosin VII in dynamic cell adhesion. Curr Biol. 2001 Mar 6;11(5):318-29. PMID:11267868
- ↑ Tuxworth RI, Stephens S, Ryan ZC, Titus MA. Identification of a myosin VII-talin complex. J Biol Chem. 2005 Jul 15;280(28):26557-64. Epub 2005 Apr 11. PMID:15826949 doi:http://dx.doi.org/M503699200
- ↑ Wang Q, Deloia MA, Kang Y, Litchke C, Zhang N, Titus MA, Walters KJ. The SH3 domain of a M7 interacts with its C-terminal proline-rich region. Protein Sci. 2007 Feb;16(2):189-96. Epub 2006 Dec 22. PMID:17189480 doi:10.1110/ps.062496807
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