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[[Image:1b5f.png|left|200px]]


{{STRUCTURE_1b5f| PDB=1b5f | SCENE= }}
==NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.==
<StructureSection load='1b5f' size='340' side='right'caption='[[1b5f]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1b5f]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cynara_cardunculus Cynara cardunculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B5F 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]] 1.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1b5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b5f OCA], [https://pdbe.org/1b5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b5f RCSB], [https://www.ebi.ac.uk/pdbsum/1b5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b5f ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARDA_CYNCA CARDA_CYNCA] Aspartic proteinase with a high preference for bonds between hydrophobic residues. Cleaves alpha-lactalbumin but not beta-lactoglobulin.[UniProtKB:P85136]<ref>PMID:16428617</ref> <ref>PMID:8654427</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/b5/1b5f_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=1b5f ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aspartic proteinases (AP) have been widely studied within the living world, but so far no plant AP have been structurally characterized. The refined cardosin A crystallographic structure includes two molecules, built up by two glycosylated peptide chains (31 and 15 kDa each). The fold of cardosin A is typical within the AP family. The glycosyl content is described by 19 sugar rings attached to Asn-67 and Asn-257. They are localized on the molecular surface away from the conserved active site and show a new glycan of the plant complex type. A hydrogen bond between Gln-126 and Manbeta4 renders the monosaccharide oxygen O-2 sterically inaccessible to accept a xylosyl residue, therefore explaining the new type of the identified plant glycan. The Arg-Gly-Asp sequence, which has been shown to be involved in recognition of a putative cardosin A receptor, was found in a loop between two beta-strands on the molecular surface opposite the active site cleft. Based on the crystal structure, a possible mechanism whereby cardosin A might be orientated at the cell surface of the style to interact with its putative receptor from pollen is proposed. The biological implications of these findings are also discussed.


===NATIVE CARDOSIN A FROM CYNARA CARDUNCULUS L.===
Crystal structure of cardosin A, a glycosylated and Arg-Gly-Asp-containing aspartic proteinase from the flowers of Cynara cardunculus L.,Frazao C, Bento I, Costa J, Soares CM, Verissimo P, Faro C, Pires E, Cooper J, Carrondo MA J Biol Chem. 1999 Sep 24;274(39):27694-701. PMID:10488111<ref>PMID:10488111</ref>


{{ABSTRACT_PUBMED_10488111}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 1b5f" style="background-color:#fffaf0;"></div>
[[1b5f]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cynara_cardunculus Cynara cardunculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B5F OCA].
== References ==
 
<references/>
==Reference==
__TOC__
<ref group="xtra">PMID:010488111</ref><references group="xtra"/>
</StructureSection>
[[Category: Cynara cardunculus]]
[[Category: Cynara cardunculus]]
[[Category: Bento, I.]]
[[Category: Large Structures]]
[[Category: Carrondo, M A.]]
[[Category: Bento I]]
[[Category: Frazao, C.]]
[[Category: Carrondo MA]]
[[Category: Aspartic proteinase]]
[[Category: Frazao C]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/1b5f"