1gd5
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gd5 OCA], [http://www.ebi.ac.uk/pdbsum/1gd5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gd5 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation. | The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation. | ||
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| - | ==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== | ==About this Structure== | ||
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[[Category: Kohda, D.]] | [[Category: Kohda, D.]] | ||
[[Category: Sumimoto, H.]] | [[Category: Sumimoto, H.]] | ||
| - | [[Category: alpha beta | + | [[Category: alpha beta,p47-phox,px domain]] |
| - | + | ||
| - | + | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:41:47 2008'' |
Revision as of 17:41, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE PX DOMAIN FROM HUMAN P47PHOX NADPH OXIDASE
Overview
The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phox protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation.
About this Structure
1GD5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the PX domain, a target of the SH3 domain., Hiroaki H, Ago T, Ito T, Sumimoto H, Kohda D, Nat Struct Biol. 2001 Jun;8(6):526-30. PMID:11373621
Page seeded by OCA on Sun Mar 30 20:41:47 2008
