4ihz

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of CrataBL, a trypsin inhibitor from Crataeva tapia

Structural highlights

4ihz is a 2 chain structure with sequence from Crateva tapia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.5Å
Ligands:	, , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LECB1_CRATA Glucose and N-acetylglucosamine binding lectin. Has hemagglutinating activity against human and rabbit erythrocytes which does not require divalent cations. Inhibits factor Xa and, to a lesser extent, trypsin. Does not inhibit neutrophil elastase, human plasma kallikrein, papain, human plasmin, porcine pancreatic kallikrein and bovin chymotrypsin. Has insecticidal activity against the termite species N.corniger. Induces apoptosis in prostrate cancer cell lines DU145 and PC3.^[1] ^[2]

Publication Abstract from PubMed

A protein isolated from the bark of Crataeva tapia (CrataBL) is both a Kunitz-type plant protease inhibitor and a lectin. We have determined the amino acid sequence and three-dimensional structure of CrataBL, as well as characterized its selected biochemical and biological properties. We found two different isoforms of CrataBL isolated from the original source, differing in positions 31 (Pro/Leu); 92 (Ser/Leu); 93 (Ile/Thr); 95 (Arg/Gly) and 97 (Leu/Ser). CrataBL showed relatively weak inhibitory activity against trypsin (Kiapp = 43 microM) and was more potent against Factor Xa (Kiapp = 8.6 microM), but was not active against a number of other proteases. We have confirmed that CrataBL contains two glycosylation sites and forms a dimer at high concentration. The high-resolution crystal structures of two different crystal forms of isoform II verified the beta-trefoil fold of CrataBL and have shown the presence of dimers consisting of two almost identical molecules making extensive contacts ( approximately 645 A2). The structure differs from those of the most closely related proteins by the lack of the N-terminal beta-hairpin. In experiments aimed at investigating the biological properties of CrataBL, we have shown that addition of 40 microM of the protein for 48 h caused maximum growth inhibition in MTT assay (47% of DU145 cells and 43% of PC3 cells). The apoptosis of DU145 and PC3 cell lines was confirmed by flow cytometry using Annexin V/FITC and propidium iodide staining. Treatment with CrataBL resulted in the release of mitochondrial cytochrome c and in the activation of caspase-3 in DU145 and PC3 cells.

Crystal Structure of Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines.,Ferreira RD, Zhou D, Ferreira JG, Silva MC, Silva-Lucca RA, Mentele R, Paredes-Gamero EJ, Bertolin TC, Dos Santos Correia MT, Paiva PM, Gustchina A, Wlodawer A, Oliva ML PLoS One. 2013 Jun 18;8(6):e64426. Print 2013. PMID:23823708^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Araujo RM, Ferreira Rda S, Napoleao TH, Carneiro-da-Cunha Md, Coelho LC, Correia MT, Oliva ML, Paiva PM. Crataeva tapia bark lectin is an affinity adsorbent and insecticidal agent. Plant Sci. 2012 Feb;183:20-6. doi: 10.1016/j.plantsci.2011.10.018. Epub 2011 Nov , 4. PMID:22195573 doi:http://dx.doi.org/10.1016/j.plantsci.2011.10.018
↑ Ferreira RD, Zhou D, Ferreira JG, Silva MC, Silva-Lucca RA, Mentele R, Paredes-Gamero EJ, Bertolin TC, Dos Santos Correia MT, Paiva PM, Gustchina A, Wlodawer A, Oliva ML. Crystal Structure of Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines. PLoS One. 2013 Jun 18;8(6):e64426. Print 2013. PMID:23823708 doi:10.1371/journal.pone.0064426
↑ Ferreira RD, Zhou D, Ferreira JG, Silva MC, Silva-Lucca RA, Mentele R, Paredes-Gamero EJ, Bertolin TC, Dos Santos Correia MT, Paiva PM, Gustchina A, Wlodawer A, Oliva ML. Crystal Structure of Bark Protein (CrataBL) and Its Effect in Human Prostate Cancer Cell Lines. PLoS One. 2013 Jun 18;8(6):e64426. Print 2013. PMID:23823708 doi:10.1371/journal.pone.0064426

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ihz"

Categories: Crateva tapia | Large Structures | Wlodawer A | Zhou D

@@ Line 1: / Line 1: @@
 ==Crystal structure of CrataBL, a trypsin inhibitor from Crataeva tapia==
-<StructureSection load='4ihz' size='340' side='right' caption='[[4ihz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
+<StructureSection load='4ihz' size='340' side='right'caption='[[4ihz]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ihz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crateva_tapia Crateva tapia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IHZ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ihz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Crateva_tapia Crateva tapia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IHZ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ii0|4ii0]]</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=4ihz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihz OCA], [https://pdbe.org/4ihz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ihz RCSB], [https://www.ebi.ac.uk/pdbsum/4ihz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihz ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ihz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ihz OCA], [http://pdbe.org/4ihz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ihz RCSB], [http://www.ebi.ac.uk/pdbsum/4ihz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ihz ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/LECB1_CRATA LECB1_CRATA] Glucose and N-acetylglucosamine binding lectin. Has hemagglutinating activity against human and rabbit erythrocytes which does not require divalent cations. Inhibits factor Xa and, to a lesser extent, trypsin. Does not inhibit neutrophil elastase, human plasma kallikrein, papain, human plasmin, porcine pancreatic kallikrein and bovin chymotrypsin. Has insecticidal activity against the termite species N.corniger. Induces apoptosis in prostrate cancer cell lines DU145 and PC3.<ref>PMID:22195573</ref> <ref>PMID:23823708</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 24: @@
 </StructureSection>
 [[Category: Crateva tapia]]
-[[Category: Wlodawer, A]]
+[[Category: Large Structures]]
-[[Category: Zhou, D]]
+[[Category: Wlodawer A]]
-[[Category: Beta-trefoil]]
+[[Category: Zhou D]]
-[[Category: Hydrolase inhibitor]]
-[[Category: Serine protease inhibitor]]

4ihz

From Proteopedia

Current revision

Crystal structure of CrataBL, a trypsin inhibitor from Crataeva tapia

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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