1sko: Difference between revisions

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New page: left|200px<br /> <applet load="1sko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sko, resolution 2.00Å" /> '''MP1-p14 Complex'''<...
 
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[[Image:1sko.gif|left|200px]]<br />
<applet load="1sko" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1sko, resolution 2.00&Aring;" />
'''MP1-p14 Complex'''<br />


==Overview==
==MP1-p14 Complex==
Scaffold proteins of the mitogen-activated protein kinase (MAPK) pathway, have been proposed to form an active signaling module and enhance the, specificity of the transduced signal. Here, we report a 2-A resolution, structure of the MAPK scaffold protein MP1 in a complex with its partner, protein, p14, that localizes the complex to late endosomes. The structures, of these two proteins are remarkably similar, with a five-stranded, beta-sheet flanked on either side by a total of three helices. The, proteins form a heterodimer in solution and interact mainly through the, edge beta-strand in each protein to generate a 10-stranded beta-sheet, core. Both proteins also share structural similarity with the, amino-terminal regulatory domains of the membrane trafficking proteins, sec22b and Ykt6p, as well as with sedlin (a component of a, Golgi-associated membrane-trafficking complex) and the sigma2 and, amino-terminal portion of the mu2 subunits of the clathrin adaptor complex, AP2. Because neither MP1 nor p14 have been implicated in membrane traffic, we propose that the similar protein folds allow these relatively small, proteins to be involved in multiple and simultaneous protein-protein, interactions. Mapping of highly conserved, surface-exposed residues on MP1, and p14 provided insight into the potential sites of binding of the, signaling kinases MEK1 and ERK1 to this complex, as well as the areas, potentially involved in other protein-protein interactions.
<StructureSection load='1sko' size='340' side='right'caption='[[1sko]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1sko]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SKO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SKO 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&#8491;</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=1sko FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sko OCA], [https://pdbe.org/1sko PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sko RCSB], [https://www.ebi.ac.uk/pdbsum/1sko PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sko ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LTOR3_HUMAN LTOR3_HUMAN] As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.<ref>PMID:20381137</ref> <ref>PMID:22980980</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/sk/1sko_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=1sko ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1SKO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SKO OCA].
*[[Mitogen-activated protein kinase kinase 3D structures|Mitogen-activated protein kinase kinase 3D structures]]
 
== References ==
==Reference==
<references/>
The structure of the MAPK scaffold, MP1, bound to its partner, p14. A complex with a critical role in endosomal map kinase signaling., Lunin VV, Munger C, Wagner J, Ye Z, Cygler M, Sacher M, J Biol Chem. 2004 May 28;279(22):23422-30. Epub 2004 Mar 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15016825 15016825]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Cygler M]]
[[Category: Cygler, M.]]
[[Category: Lunin VV]]
[[Category: Lunin, V.V.]]
[[Category: Munger C]]
[[Category: Munger, C.]]
[[Category: Sacher M]]
[[Category: Sacher, M.]]
[[Category: Wagner J]]
[[Category: Wagner, J.]]
[[Category: Ye Z]]
[[Category: Ye, Z.]]
[[Category: map kinase pathway]]
[[Category: mp1-p14 complex]]
[[Category: scaffold proteins]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:15:03 2007''

Latest revision as of 11:31, 14 February 2024

MP1-p14 ComplexMP1-p14 Complex

Structural highlights

1sko is a 2 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LTOR3_HUMAN As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Sancak Y, Bar-Peled L, Zoncu R, Markhard AL, Nada S, Sabatini DM. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell. 2010 Apr 16;141(2):290-303. doi: 10.1016/j.cell.2010.02.024. Epub 2010 Apr , 8. PMID:20381137 doi:10.1016/j.cell.2010.02.024
  2. ↑ Bar-Peled L, Schweitzer LD, Zoncu R, Sabatini DM. Ragulator is a GEF for the rag GTPases that signal amino acid levels to mTORC1. Cell. 2012 Sep 14;150(6):1196-208. doi: 10.1016/j.cell.2012.07.032. PMID:22980980 doi:10.1016/j.cell.2012.07.032

1sko, resolution 2.00Å

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