3h32

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[[Image:3h32.png|left|200px]]
 
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==Crystal structure of D-dimer from human fibrin complexed with Gly-His-Arg-Pro-Tyr-amide==
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The line below this paragraph, containing "STRUCTURE_3h32", creates the "Structure Box" on the page.
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<StructureSection load='3h32' size='340' side='right'caption='[[3h32]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3h32]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3H32 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
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{{STRUCTURE_3h32| PDB=3h32 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3h32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h32 OCA], [https://pdbe.org/3h32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3h32 RCSB], [https://www.ebi.ac.uk/pdbsum/3h32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3h32 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/FIBA_HUMAN FIBA_HUMAN] Defects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:[https://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:[https://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>
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== Function ==
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[https://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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/3h32_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3h32 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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When fibrin clots are formed in vitro in the presence of certain positively charged peptides, the turbidity is enhanced and fibrinolysis is delayed. Here we show that these two phenomena are not always linked and that different families of peptides bring about the delay of lysis in different ways. In the case of intrinsically adhesive peptides corresponding to certain regions of the fibrinogen gammaC and betaC domains, even though these peptides bind to fibrin(ogen) and enhance turbidity, the delay in lysis is mainly due to direct inhibition of plasminogen activation. In contrast, for certain pentapeptides patterned on fibrin B knobs, the delay in lysis is a consequence of how fibrin units assemble. On their own, these B knob surrogates can induce the gelation of fibrinogen molecules. The likely cause of enhanced clot turbidity and delay in fibrinolysis was revealed by a crystal structure of the D-dimer from human fibrinogen cocrystallized with GHRPYam, the packing of which showed the direct involvement of the ligand tyrosines in antiparallel betaC-betaC interactions.
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===Crystal structure of D-dimer from human fibrin complexed with Gly-His-Arg-Pro-Tyr-amide===
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Two Families of Synthetic Peptides That Enhance Fibrin Turbidity and Delay Fibrinolysis by Different Mechanisms.,Pandi L, Kollman JM, Lopez-Lira F, Burrows JM, Riley M, Doolittle RF Biochemistry. 2009 Jul 9. PMID:19588915<ref>PMID:19588915</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3h32" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19588915 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19588915}}
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==About this Structure==
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[[3h32]] is a 8 chain structure of [[Fibrin]] and [[Fibrinogen]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3H32 OCA].
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==See Also==
==See Also==
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*[[Fibrin]]
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*[[Fibrin|Fibrin]]
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*[[Fibrinogen]]
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*[[Fibrinogen|Fibrinogen]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:019588915</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Doolittle, R F.]]
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[[Category: Large Structures]]
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[[Category: Pandi, L.]]
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[[Category: Doolittle RF]]
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[[Category: Alternative splicing]]
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[[Category: Pandi L]]
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[[Category: Amyloid]]
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[[Category: Amyloidosis]]
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[[Category: Blood clotting]]
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[[Category: Blood coagulation]]
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[[Category: Calcium]]
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[[Category: Cdna flj75335]]
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[[Category: Coiled coil]]
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[[Category: Disease mutation]]
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[[Category: Disulfide bond]]
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[[Category: Fibrin clot]]
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[[Category: Fibrinogen]]
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[[Category: Glycoprotein]]
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[[Category: Isoform cra_m]]
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[[Category: Isopeptide bond]]
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[[Category: Mrna]]
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[[Category: Phosphoprotein]]
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[[Category: Polymorphism]]
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[[Category: Pyrrolidone carboxylic acid]]
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[[Category: Secreted]]
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[[Category: Sulfation]]
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[[Category: Transcript variant gamma-a]]
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Current revision

Crystal structure of D-dimer from human fibrin complexed with Gly-His-Arg-Pro-Tyr-amide

PDB ID 3h32

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