1qmt

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{{Seed}}
 
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[[Image:1qmt.png|left|200px]]
 
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==Recombinant Human Eosinophil Cationic Protein==
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The line below this paragraph, containing "STRUCTURE_1qmt", creates the "Structure Box" on the page.
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<StructureSection load='1qmt' size='340' side='right'caption='[[1qmt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1qmt]] 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=1QMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMT FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=1qmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmt OCA], [https://pdbe.org/1qmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmt RCSB], [https://www.ebi.ac.uk/pdbsum/1qmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmt ProSAT]</span></td></tr>
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{{STRUCTURE_1qmt| PDB=1qmt | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ECP_HUMAN ECP_HUMAN] Cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. Possesses a wide variety of biological activities. Exhibits antibacterial activity, including cytoplasmic membrane depolarization of preferentially Gram-negative, but also Gram-positive strains. Promotes E.coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.<ref>PMID:2501794</ref> <ref>PMID:19450231</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/qm/1qmt_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=1qmt 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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Eosinophil cationic protein (ECP) is located in the matrix of the eosinophil's large specific granule and has marked toxicity for a variety of helminth parasites, hemoflagellates, bacteria, single-stranded RNA virus, and mammalian cells and tissues. It belongs to the bovine pancreatic ribonuclease A (RNase A) family and exhibits ribonucleolytic activity which is about 100-fold lower than that of a related eosinophil ribonuclease, the eosinophil-derived neurotoxin (EDN). The crystal structure of human ECP, determined at 2.4 A, is similar to that of RNase A and EDN. It reveals that residues Gln-14, His-15, Lys-38, Thr-42, and His-128 at the active site are conserved as in all other RNase A homologues. Nevertheless, evidence for considerable divergence of ECP is also implicit in the structure. Amino acid residues Arg-7, Trp-10, Asn-39, His-64, and His-82 appear to play a key part in the substrate specificity and low catalytic activity of ECP. The structure also shows how the cationic residues are distributed on the surface of the ECP molecule that may have implications for an understanding of the cytotoxicity of this enzyme.
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===RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN===
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Crystal structure of eosinophil cationic protein at 2.4 A resolution.,Boix E, Leonidas DD, Nikolovski Z, Nogues MV, Cuchillo CM, Acharya KR Biochemistry. 1999 Dec 21;38(51):16794-801. PMID:10606511<ref>PMID:10606511</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>
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<div class="pdbe-citations 1qmt" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_10606511}}, adds the Publication Abstract to the page
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*[[Protein G|Protein G]]
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(as it appears on PubMed at http://www.pubmed.gov), where 10606511 is the PubMed ID number.
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_10606511}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1QMT is a 1 chain structure of 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=1QMT OCA].
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==Reference==
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<ref group="xtra">PMID:10606511</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Acharya, K R.]]
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[[Category: Large Structures]]
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[[Category: Boix, E.]]
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[[Category: Acharya KR]]
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[[Category: Leonidas, D D.]]
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[[Category: Boix E]]
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[[Category: Cytotoxicity]]
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[[Category: Leonidas DD]]
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[[Category: Eosinophil]]
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[[Category: Ribonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:56:23 2009''
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Current revision

Recombinant Human Eosinophil Cationic Protein

PDB ID 1qmt

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