1w0r
From Proteopedia
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{{STRUCTURE_1w0r| PDB=1w0r | SCENE= }} | {{STRUCTURE_1w0r| PDB=1w0r | SCENE= }} | ||
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===SOLUTION STRUCTURE OF DIMERIC FORM OF PROPERDIN BY X-RAY SOLUTION SCATTERING AND ANALYTICAL ULTRACENTRIFUGATION=== | ===SOLUTION STRUCTURE OF DIMERIC FORM OF PROPERDIN BY X-RAY SOLUTION SCATTERING AND ANALYTICAL ULTRACENTRIFUGATION=== | ||
| + | {{ABSTRACT_PUBMED_15491616}} | ||
| - | + | ==Disease== | |
| + | [[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:[http://omim.org/entry/312060 312060]]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).<ref>PMID:8871668</ref><ref>PMID:9710744</ref><ref>PMID:10909851</ref> | ||
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| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/PROP_HUMAN PROP_HUMAN]] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. | ||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID:015491616</ref><references group="xtra"/> | + | <ref group="xtra">PMID:015491616</ref><references group="xtra"/><references/> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Perkins, S J.]] | [[Category: Perkins, S J.]] | ||
Revision as of 03:55, 25 March 2013
Contents |
SOLUTION STRUCTURE OF DIMERIC FORM OF PROPERDIN BY X-RAY SOLUTION SCATTERING AND ANALYTICAL ULTRACENTRIFUGATION
Template:ABSTRACT PUBMED 15491616
Disease
[PROP_HUMAN] Defects in CFP are the cause of properdin deficiency (PFD) [MIM:312060]. PFD results in higher susceptibility to bacterial infections; especially to meningococcal infections. Three phenotypes have been reported: complete deficiency (type I), incomplete deficiency (type II), and dysfunction of properdin (type III).[1][2][3]
Function
[PROP_HUMAN] A positive regulator of the alternate pathway of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes.
About this Structure
1w0r is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Sun Z, Reid KB, Perkins SJ. The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling. J Mol Biol. 2004 Nov 5;343(5):1327-43. PMID:15491616 doi:http://dx.doi.org/10.1016/j.jmb.2004.09.001
- ↑ Fredrikson GN, Westberg J, Kuijper EJ, Tijssen CC, Sjoholm AG, Uhlen M, Truedsson L. Molecular characterization of properdin deficiency type III: dysfunction produced by a single point mutation in exon 9 of the structural gene causing a tyrosine to aspartic acid interchange. J Immunol. 1996 Oct 15;157(8):3666-71. PMID:8871668
- ↑ Fredrikson GN, Gullstrand B, Westberg J, Sjoholm AG, Uhlen M, Truedsson L. Expression of properdin in complete and incomplete deficiency: normal in vitro synthesis by monocytes in two cases with properdin deficiency type II due to distinct mutations. J Clin Immunol. 1998 Jul;18(4):272-82. PMID:9710744
- ↑ van den Bogaard R, Fijen CA, Schipper MG, de Galan L, Kuijper EJ, Mannens MM. Molecular characterisation of 10 Dutch properdin type I deficient families: mutation analysis and X-inactivation studies. Eur J Hum Genet. 2000 Jul;8(7):513-8. PMID:10909851 doi:10.1038/sj.ejhg.5200496
