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[[Image:1qmt.gif|left|200px]]
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{{STRUCTURE_1qmt|  PDB=1qmt  |  SCENE=  }}
'''RECOMBINANT HUMAN EOSINOPHIL CATIONIC PROTEIN'''


==Recombinant Human Eosinophil Cationic Protein==
<StructureSection load='1qmt' size='340' side='right'caption='[[1qmt]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>
== 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/qm/1qmt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1qmt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1QMT is a [[Single protein]] 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].
</div>
<div class="pdbe-citations 1qmt" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/10606511 10606511]
*[[Protein G|Protein G]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Acharya, K R.]]
[[Category: Acharya KR]]
[[Category: Boix, E.]]
[[Category: Boix E]]
[[Category: Leonidas, D D.]]
[[Category: Leonidas DD]]
[[Category: Cytotoxicity]]
[[Category: Eosinophil]]
[[Category: Ribonuclease]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:27:46 2008''
Retrieved from "https://proteopedia.org/1qmt"