1q0p: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
New page: left|200px<br /> <applet load="1q0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q0p, resolution 1.8Å" /> '''A domain of Factor B...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
 
(16 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1q0p.gif|left|200px]]<br />
<applet load="1q0p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1q0p, resolution 1.8&Aring;" />
'''A domain of Factor B'''<br />


==Overview==
==A domain of Factor B==
Complement factor B is a 90 kDa protein consisting of three domains: a, three-module complement control protein, a von Willebrand factor A domain, and a C-terminal serine protease (SP) domain that adopts a default, inactive (zymogen) conformation. The interaction between factor B and, pathogen-bound C3b is mediated by its A domain, triggering a, conformational change in factor B that ultimately creates the "C3, convertase" of the alternative complement pathway. We report the crystal, structure of the A domain from factor B and show that it contains an, integrin-like MIDAS motif that adopts the "open" conformation typical of, integrin-ligand complexes, with an acidic residue (provided by a, fortuitous crystal contact) completing the coordination of the metal ion., Modeling studies indicate that the factor B A domain can also adopt the, closed conformation, supporting the hypothesis that an "integrin-like, switch" is conserved in complement proteins and perhaps in 60 other A, domains found within the human proteome.
<StructureSection load='1q0p' size='340' side='right'caption='[[1q0p]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1q0p]] 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=1Q0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q0P FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q0p OCA], [https://pdbe.org/1q0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q0p RCSB], [https://www.ebi.ac.uk/pdbsum/1q0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q0p ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN] Defects in CFB are a cause of susceptibility to hemolytic uremic syndrome atypical type 4 (AHUS4) [MIM:[https://omim.org/entry/612924 612924]. An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Note=Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype.<ref>PMID:17182750</ref> <ref>PMID:20513133</ref>
== Function ==
[https://www.uniprot.org/uniprot/CFAB_HUMAN CFAB_HUMAN] Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. It has also been implicated in proliferation and differentiation of preactivated B-lymphocytes, rapid spreading of peripheral blood monocytes, stimulation of lymphocyte blastogenesis and lysis of erythrocytes. Ba inhibits the proliferation of preactivated B-lymphocytes.
== 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/q0/1q0p_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=1q0p ConSurf].
<div style="clear:both"></div>


==Disease==
==See Also==
Known diseases associated with this structure: Macular degeneration, age-related, reduced risk of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=138470 138470]]
*[[Complement factor 3D structures|Complement factor 3D structures]]
 
== References ==
==About this Structure==
<references/>
1Q0P 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 MN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alternative-complement-pathway_C3/C5_convertase Alternative-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.47 3.4.21.47] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q0P OCA].
__TOC__
 
</StructureSection>
==Reference==
Crystal structure of the A domain from complement factor B reveals an integrin-like open conformation., Bhattacharya AA, Lupher ML Jr, Staunton DE, Liddington RC, Structure. 2004 Mar;12(3):371-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15016353 15016353]
[[Category: Alternative-complement-pathway C3/C5 convertase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bhattacharya, A.A.]]
[[Category: Bhattacharya AA]]
[[Category: Liddington, R.C.]]
[[Category: Liddington RC]]
[[Category: MN]]
[[Category: a domain]]
[[Category: factor b]]
[[Category: i domain]]
[[Category: mac-1]]
[[Category: von willebrand factor]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:49:16 2007''
Retrieved from "https://proteopedia.org/1q0p"