1xa6: Difference between revisions

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New page: left|200px<br /> <applet load="1xa6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xa6, resolution 3.2Å" /> '''Crystal Structure of...
 
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[[Image:1xa6.gif|left|200px]]<br />
<applet load="1xa6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1xa6, resolution 3.2&Aring;" />
'''Crystal Structure of the Human Beta2-Chimaerin'''<br />


==Overview==
==Crystal Structure of the Human Beta2-Chimaerin==
The lipid second messenger diacylglycerol acts by binding to the C1, domains of target proteins, which translocate to cell membranes and are, allosterically activated. Here we report the crystal structure at 3.2 A, resolution of one such protein, beta2-chimaerin, a GTPase-activating, protein for the small GTPase Rac, in its inactive conformation. The, structure shows that in the inactive state, the N terminus of, beta2-chimaerin protrudes into the active site of the RacGAP domain, sterically blocking Rac binding. The diacylglycerol and phospholipid, membrane binding site on the C1 domain is buried by contacts with the four, different regions of beta2-chimaerin: the N terminus, SH2 domain, RacGAP, domain, and the linker between the SH2 and C1 domains. Phospholipid, binding to the C1 domain triggers the cooperative dissociation of these, interactions, allowing the N terminus to move out of the active site and, thereby activating the enzyme.
<StructureSection load='1xa6' size='340' side='right'caption='[[1xa6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 
== Structural highlights ==
==Disease==
<table><tr><td colspan='2'>[[1xa6]] is a 1 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=1XA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XA6 FirstGlance]. <br>
Known disease associated with this structure: Apnea, postanesthetic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=177400 177400]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xa6 OCA], [https://pdbe.org/1xa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xa6 RCSB], [https://www.ebi.ac.uk/pdbsum/1xa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xa6 ProSAT]</span></td></tr>
1XA6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XA6 OCA].
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/CHIO_HUMAN CHIO_HUMAN] GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.
Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin., Canagarajah B, Leskow FC, Ho JY, Mischak H, Saidi LF, Kazanietz MG, Hurley JH, Cell. 2004 Oct 29;119(3):407-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15507211 15507211]
== 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/xa/1xa6_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=1xa6 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Canagarajah, B.]]
[[Category: Canagarajah B]]
[[Category: Ho, J.Y.]]
[[Category: Ho JY]]
[[Category: Hurley, J.H.]]
[[Category: Hurley JH]]
[[Category: Kazanietz, M.G.]]
[[Category: Kazanietz MG]]
[[Category: Leskow, F.C.]]
[[Category: Leskow FC]]
[[Category: Mischak, H.]]
[[Category: Mischak H]]
[[Category: Saidi, L.F.]]
[[Category: Saidi LF]]
[[Category: ZN]]
[[Category: beta2-chimaerin]]
[[Category: c1]]
[[Category: racgap]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:02:44 2007''

Latest revision as of 11:48, 14 February 2024

Crystal Structure of the Human Beta2-ChimaerinCrystal Structure of the Human Beta2-Chimaerin

Structural highlights

1xa6 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CHIO_HUMAN GTPase-activating protein for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors.

Evolutionary Conservation

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

1xa6, resolution 3.20Å

Drag the structure with the mouse to rotate

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