4f27: Difference between revisions

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 ==Crystal structures reveal the multi-ligand binding mechanism of the Staphylococcus aureus ClfB==
-<StructureSection load='4f27' size='340' side='right' caption='[[4f27]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
+<StructureSection load='4f27' size='340' side='right'caption='[[4f27]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4f27]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F27 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F27 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4f27]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MRSA252 Staphylococcus aureus subsp. aureus MRSA252]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F27 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.917&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4f1z|4f1z]], [[4f20|4f20]], [[4f24|4f24]]</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=4f27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f27 OCA], [https://pdbe.org/4f27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f27 RCSB], [https://www.ebi.ac.uk/pdbsum/4f27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f27 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">clfB, SAR2709 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 Staphylococcus aureus])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4f27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f27 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f27 RCSB], [http://www.ebi.ac.uk/pdbsum/4f27 PDBsum]</span></td></tr>
 </table>
-== Disease ==
-[[http://www.uniprot.org/uniprot/FIBA_HUMAN FIBA_HUMAN]] Defects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:[http://omim.org/entry/202400 202400]]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.  Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8097946</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/FIBA_HUMAN FIBA_HUMAN]] Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
+[https://www.uniprot.org/uniprot/CLFB_STAAR CLFB_STAAR] Cell surface-associated protein implicated in virulence by promoting bacterial attachment to both alpha- and beta-chains of human fibrinogen and inducing the formation of bacterial clumps.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4f27" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 28: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Staphylococcus aureus]]
+[[Category: Homo sapiens]]
-[[Category: Chen, Y G]]
+[[Category: Large Structures]]
-[[Category: Deng, X M]]
+[[Category: Staphylococcus aureus subsp. aureus MRSA252]]
-[[Category: Feng, Y]]
+[[Category: Chen YG]]
-[[Category: Liu, B]]
+[[Category: Deng XM]]
-[[Category: Liu, L]]
+[[Category: Feng Y]]
-[[Category: Wang, J W]]
+[[Category: Liu B]]
-[[Category: Xiang, H]]
+[[Category: Liu L]]
-[[Category: Yang, M J]]
+[[Category: Wang JW]]
-[[Category: Cell adhesion-blood clotting complex]]
+[[Category: Xiang H]]
-[[Category: Cell surface]]
+[[Category: Yang MJ]]
-[[Category: Dev-igg fold]]
-[[Category: Fibronogen]]
-[[Category: Protein-peptide complex]]