1oey: Difference between revisions

Revision as of 10:07, 1 November 2017

Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase

Structural highlights

1oey is a 8 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	MSE
Related:	1e96, 1hh8, 1ip9, 1ipg, 1k4u, 1h6h
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Maximal activation of NADPH oxidase requires formation of a complex between the p40(phox) and p67(phox) subunits via association of their PB1 domains. We have determined the crystal structure of the p40(phox)/p67(phox) PB1 heterodimer, which reveals that both domains have a beta grasp topology and that they bind in a front-to-back arrangement through conserved electrostatic interactions between an acidic OPCA motif on p40(phox) and basic residues in p67(phox). The structure enabled us to identify residues critical for heterodimerization among other members of the PB1 domain family, including the atypical protein kinase C zeta (PKC zeta) and its partners Par6 and p62 (ZIP, sequestosome). Both Par6 and p62 use their basic "back" to interact with the OPCA motif on the "front" of the PKC zeta. Besides heterodimeric interactions, some PB1 domains, like the p62 PB1, can make homotypic front-to-back arrays.

PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62.,Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL Mol Cell. 2003 Jul;12(1):39-50. PMID:12887891^[1]

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

References

↑ Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL. PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell. 2003 Jul;12(1):39-50. PMID:12887891

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OCA

[1] Wilson MI, Gill DJ, Perisic O, Quinn MT, Williams RL. PB1 domain-mediated heterodimerization in NADPH oxidase and signaling complexes of atypical protein kinase C with Par6 and p62. Mol Cell. 2003 Jul;12(1):39-50. PMID:12887891

[1]

@@ Line 1: / Line 1: @@
-==HETERODIMER OF P40PHOX AND P67PHOX PB1 DOMAINS FROM HUMAN NADPH OXIDASE==
+==Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase==
 <StructureSection load='1oey' size='340' side='right' caption='[[1oey]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e96|1e96]], [[1hh8|1hh8]], [[1ip9|1ip9]], [[1ipg|1ipg]], [[1k4u|1k4u]], [[1h6h|1h6h]]</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=1oey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oey OCA], [http://pdbe.org/1oey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oey RCSB], [http://www.ebi.ac.uk/pdbsum/1oey 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=1oey FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oey OCA], [http://pdbe.org/1oey PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oey RCSB], [http://www.ebi.ac.uk/pdbsum/1oey PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oey ProSAT]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/NCF4_HUMAN NCF4_HUMAN]] Defects in NCF4 are the cause of chronic granulomatous disease autosomal recessive cytochrome-b-positive type 3 (CGD3) [MIM:[http://omim.org/entry/613960 613960]]. CGD3 is a disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.<ref>PMID:19692703</ref>
-== Function ==
-[[http://www.uniprot.org/uniprot/NCF4_HUMAN NCF4_HUMAN]] Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 16: @@
      <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1oey ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1oey: Difference between revisions

Revision as of 10:07, 1 November 2017

Heterodimer of p40phox and p67phox PB1 domains from human NADPH oxidase

Structural highlights

Evolutionary Conservation

Publication Abstract from PubMed

References

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