1c1y: Difference between revisions

New page: left|200px<br /> <applet load="1c1y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1y, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1c1y.gif|left|200px]]<br />
<applet load="1c1y" size="450" color="white" frame="true" align="right" spinBox="true"
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'''CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).'''<br />


==Overview==
==CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).==
The X-ray crystal structure of the complex between the Ras-related protein, Rap1A in the GTP-analogue (GppNHp) form and the Ras-binding domain (RBD), of the Ras effector molecule c-Raf1, a Ser/Thr-specific protein kinase, has been solved to a resolution of 2.2 A. It shows that RBD has the, ubiquitin superfold and that the structure of Rap1A is very similar to, that of Ras. The interaction between the two proteins is mediated by an, apparent central antiparallel beta-sheet formed by strands B1-B2 from RBD, and strands beta 2-beta 3 from Rap1A. Complex formation is mediated by, main-chain and side-chain interactions of the so-called effector residues, in the switch I region of Rap1A.
<StructureSection load='1c1y' size='340' side='right'caption='[[1c1y]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1c1y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1Y 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=1c1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1y OCA], [https://pdbe.org/1c1y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1y RCSB], [https://www.ebi.ac.uk/pdbsum/1c1y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1y ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RAP1A_HUMAN RAP1A_HUMAN] Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner.
== 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/c1/1c1y_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=1c1y ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1C1Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, CA and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C1Y OCA].
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue., Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A, Nature. 1995 Jun 15;375(6532):554-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7791872 7791872]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Nassar, N.]]
[[Category: Nassar N]]
[[Category: CA]]
[[Category: GTP]]
[[Category: MG]]
[[Category: effectors]]
[[Category: gtp-binding proteins]]
[[Category: protein-protein complex]]
 
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