1rhp

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(New page: 200px<br /> <applet load="1rhp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rhp, resolution 2.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1rhp.gif|left|200px]]<br />
 
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<applet load="1rhp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1rhp, resolution 2.4&Aring;" />
 
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'''CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4==
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The crystal structure of human platelet factor 4 (PF4) has been solved to, a resolution of 2.4 A by molecular replacement and refined to an R-factor, of 24.1%. The structure consists of four polypeptide chains which form a, tetrameric unit. N-terminal residues, previously defined as a random coil, or extended loop region, form antiparallel beta-sheet-like structures that, form noncovalent associations between dimers. These antiparallel, beta-sheet-like structures are positioned lateral to the beta-bilayer, motif and stabilize the tetrameric unit. A positively charged ring of, lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding., The electrostatic interactions of multiply charged amino acid side chains, and hydrogen bonding interactions at the AB/CD dimer interface serve to, stabilize the tetrameric structure further.
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<StructureSection load='1rhp' size='340' side='right'caption='[[1rhp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1rhp]] is a 4 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=1RHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RHP 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]] 2.4&#8491;</td></tr>
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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=1rhp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rhp OCA], [https://pdbe.org/1rhp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rhp RCSB], [https://www.ebi.ac.uk/pdbsum/1rhp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rhp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLF4_HUMAN PLF4_HUMAN] Released during platelet aggregation. Neutralizes the anticoagulant effect of heparin because it binds more strongly to heparin than to the chondroitin-4-sulfate chains of the carrier molecule. Chemotactic for neutrophils and monocytes. Inhibits endothelial cell proliferation, the short form is a more potent inhibitor than the longer form.<ref>PMID:7644496</ref>
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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/rh/1rhp_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=1rhp 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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The crystal structure of human platelet factor 4 (PF4) has been solved to a resolution of 2.4 A by molecular replacement and refined to an R-factor of 24.1%. The structure consists of four polypeptide chains which form a tetrameric unit. N-terminal residues, previously defined as a random coil or extended loop region, form antiparallel beta-sheet-like structures that form noncovalent associations between dimers. These antiparallel beta-sheet-like structures are positioned lateral to the beta-bilayer motif and stabilize the tetrameric unit. A positively charged ring of lysine and arginine side chains encircles the PF4 tetramer sphere, presenting multiple potential sites and orientations for heparin binding. The electrostatic interactions of multiply charged amino acid side chains and hydrogen bonding interactions at the AB/CD dimer interface serve to stabilize the tetrameric structure further.
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==About this Structure==
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Crystal structure of recombinant human platelet factor 4.,Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE Biochemistry. 1994 Jul 12;33(27):8361-6. PMID:8031770<ref>PMID:8031770</ref>
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1RHP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RHP OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of recombinant human platelet factor 4., Zhang X, Chen L, Bancroft DP, Lai CK, Maione TE, Biochemistry. 1994 Jul 12;33(27):8361-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8031770 8031770]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1rhp" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Chen, L.]]
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[[Category: Zhang, X.]]
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[[Category: platelet factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:03:59 2007''
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==See Also==
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*[[C-X-C motif chemokine 3D structures|C-X-C motif chemokine 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chen L]]
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[[Category: Zhang X]]

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CRYSTAL STRUCTURE OF RECOMBINANT HUMAN PLATELET FACTOR 4

PDB ID 1rhp

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