This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1q0p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 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...)
Current revision (08:12, 14 February 2024) (edit) (undo)
 
(16 intermediate revisions 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''
+

Current revision

A domain of Factor B

PDB ID 1q0p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q0p"
Personal tools