1ng2: Difference between revisions

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{{Seed}}
[[Image:1ng2.png|left|200px]]


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==Structure of autoinhibited p47phox==
The line below this paragraph, containing "STRUCTURE_1ng2", creates the "Structure Box" on the page.
<StructureSection load='1ng2' size='340' side='right'caption='[[1ng2]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ng2]] 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=1NG2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NG2 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ng2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ng2 OCA], [https://pdbe.org/1ng2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ng2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ng2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ng2 ProSAT]</span></td></tr>
{{STRUCTURE_1ng2|  PDB=1ng2  |  SCENE=  }}
</table>
== Disease ==
[https://www.uniprot.org/uniprot/NCF1_HUMAN NCF1_HUMAN] Defects in NCF1 are the cause of chronic granulomatous disease autosomal recessive cytochrome-b-positive type 1 (CGD1) [MIM:[https://omim.org/entry/233700 233700]. Chronic granulomatous disease is a genetically heterogeneous 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:2011585</ref> <ref>PMID:11133775</ref>
== Function ==
[https://www.uniprot.org/uniprot/NCF1_HUMAN NCF1_HUMAN] NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).<ref>PMID:19801500</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/ng/1ng2_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=1ng2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The multi-subunit NADPH oxidase complex plays a crucial role in host defense against microbial infection through the production of reactive oxygen species. Activation of the NADPH oxidase requires the targeting of a cytoplasmic p40-p47-p67(phox) complex to the membrane bound heterodimeric p22-gp91(phox) flavocytochrome. This interaction is prevented in the resting state due to an auto-inhibited conformation of p47(phox). The X-ray structure of the auto-inhibited form of p47(phox) reveals that tandem SH3 domains function together to maintain the cytoplasmic complex in an inactive form. Further structural and biochemical data show that phosphorylation of p47(phox) activates a molecular switch that relieves the inhibitory intramolecular interaction. This permits p47(phox) to interact with the cytoplasmic tail of p22(phox) and initiate formation of the active, membrane bound enzyme complex.


===Structure of autoinhibited p47phox===
Molecular basis of phosphorylation-induced activation of the NADPH oxidase.,Groemping Y, Lapouge K, Smerdon SJ, Rittinger K Cell. 2003 May 2;113(3):343-55. PMID:12732142<ref>PMID:12732142</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ng2" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_12732142}}, adds the Publication Abstract to the page
*[[NADPH oxidase 3D structures|NADPH oxidase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 12732142 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_12732142}}
__TOC__
 
</StructureSection>
==Disease==
Known disease associated with this structure: Chronic granulomatous disease due to deficiency of NCF-1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608512 608512]]
 
==About this Structure==
1NG2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NG2 OCA].
 
==Reference==
Molecular basis of phosphorylation-induced activation of the NADPH oxidase., Groemping Y, Lapouge K, Smerdon SJ, Rittinger K, Cell. 2003 May 2;113(3):343-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12732142 12732142]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Groemping, Y.]]
[[Category: Groemping Y]]
[[Category: Lapouge, K.]]
[[Category: Lapouge K]]
[[Category: Rittinger, K.]]
[[Category: Rittinger K]]
[[Category: Smerdon, S J.]]
[[Category: Smerdon SJ]]
[[Category: Autoinhibited]]
[[Category: Nadph oxidase]]
[[Category: P47phox]]
[[Category: Sh3 domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:02:15 2008''

Latest revision as of 11:53, 22 May 2024

Structure of autoinhibited p47phoxStructure of autoinhibited p47phox

Structural highlights

1ng2 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 1.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

NCF1_HUMAN Defects in NCF1 are the cause of chronic granulomatous disease autosomal recessive cytochrome-b-positive type 1 (CGD1) [MIM:233700. Chronic granulomatous disease is a genetically heterogeneous disorder characterized by the inability of neutrophils and phagocytes to kill microbes that they have ingested. Patients suffer from life-threatening bacterial/fungal infections.[1] [2]

Function

NCF1_HUMAN NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).[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

The multi-subunit NADPH oxidase complex plays a crucial role in host defense against microbial infection through the production of reactive oxygen species. Activation of the NADPH oxidase requires the targeting of a cytoplasmic p40-p47-p67(phox) complex to the membrane bound heterodimeric p22-gp91(phox) flavocytochrome. This interaction is prevented in the resting state due to an auto-inhibited conformation of p47(phox). The X-ray structure of the auto-inhibited form of p47(phox) reveals that tandem SH3 domains function together to maintain the cytoplasmic complex in an inactive form. Further structural and biochemical data show that phosphorylation of p47(phox) activates a molecular switch that relieves the inhibitory intramolecular interaction. This permits p47(phox) to interact with the cytoplasmic tail of p22(phox) and initiate formation of the active, membrane bound enzyme complex.

Molecular basis of phosphorylation-induced activation of the NADPH oxidase.,Groemping Y, Lapouge K, Smerdon SJ, Rittinger K Cell. 2003 May 2;113(3):343-55. PMID:12732142[4]

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

See Also

References

  1. ↑ Casimir CM, Bu-Ghanim HN, Rodaway AR, Bentley DL, Rowe P, Segal AW. Autosomal recessive chronic granulomatous disease caused by deletion at a dinucleotide repeat. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2753-7. PMID:2011585
  2. ↑ Noack D, Rae J, Cross AR, Ellis BA, Newburger PE, Curnutte JT, Heyworth PG. Autosomal recessive chronic granulomatous disease caused by defects in NCF-1, the gene encoding the phagocyte p47-phox: mutations not arising in the NCF-1 pseudogenes. Blood. 2001 Jan 1;97(1):305-11. PMID:11133775
  3. ↑ Kilpatrick LE, Sun S, Li H, Vary TC, Korchak HM. Regulation of TNF-induced oxygen radical production in human neutrophils: role of delta-PKC. J Leukoc Biol. 2010 Jan;87(1):153-64. doi: 10.1189/jlb.0408230. Epub 2009 Oct 2. PMID:19801500 doi:10.1189/jlb.0408230
  4. ↑ Groemping Y, Lapouge K, Smerdon SJ, Rittinger K. Molecular basis of phosphorylation-induced activation of the NADPH oxidase. Cell. 2003 May 2;113(3):343-55. PMID:12732142

1ng2, resolution 1.70Å

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