4hv3

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(Difference between revisions)

Revision as of 18:48, 1 February 2017

Structure of Ricin A chain bound with N-(N-(pterin-7-yl)carbonyl-L-serinyl)-L-tryptophan

Structural highlights

4hv3 is a 1 chain structure with sequence from Castor bean. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1rtc, 1ift, 1br6, 1px8, 1px9, 4esi, 4huo, 4hup, 4hv7
Activity:	rRNA N-glycosylase, with EC number 3.2.2.22
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RICI_RICCO] Ricin is highly toxic to animal cells and to a lesser extent to plant cells. The A chain acts as a glycosidase that removes a specific adenine residue from an exposed loop of the 28S rRNA (A4324 in mammals), leading to rRNA breakage. As this loop is involved in elongation factor binding, modified ribosomes are catalytically inactive and unable to support protein synthesis. The A chain can inactivate a few thousand ribosomes per minute, faster than the cell can make new ones. Therefore a single A chain molecule can kill an animal cell. The B chain binds to beta-D-galactopyranoside moieties on cell surface glycoproteins and glycolipids and facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (Lectin activity).

Publication Abstract from PubMed

Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as through X-ray crystallography. Despite the relatively polar, solvent exposed active site, several hydrophobic interactions, most commonly pi-interactions not predicted by modeling programs, were identified in all of the best-performing inhibitors. Nearly all of these compounds provide IC(50) values in the low micromolar range.

Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A.,Saito R, Pruet JM, Manzano LA, Jasheway K, Monzingo AF, Wiget PA, Kamat I, Anslyn EV, Robertus JD J Med Chem. 2012 Dec 19. PMID:23214944^[1]

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

References

↑ Saito R, Pruet JM, Manzano LA, Jasheway K, Monzingo AF, Wiget PA, Kamat I, Anslyn EV, Robertus JD. Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A. J Med Chem. 2012 Dec 19. PMID:23214944 doi:http://dx.doi.org/10.1021/jm3016393

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/4hv3"

@@ Line 1: / Line 1: @@
 ==Structure of Ricin A chain bound with N-(N-(pterin-7-yl)carbonyl-L-serinyl)-L-tryptophan==
 <StructureSection load='4hv3' size='340' side='right' caption='[[4hv3]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rtc|1rtc]], [[1ift|1ift]], [[1br6|1br6]], [[1px8|1px8]], [[1px9|1px9]], [[4esi|4esi]], [[4huo|4huo]], [[4hup|4hup]], [[4hv7|4hv7]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </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=4hv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hv3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hv3 PDBsum]</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=4hv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hv3 OCA], [http://pdbe.org/4hv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hv3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4hv3" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Ricin|Ricin]]
 == References ==
 <references/>

4hv3

From Proteopedia

Revision as of 18:48, 1 February 2017

Structure of Ricin A chain bound with N-(N-(pterin-7-yl)carbonyl-L-serinyl)-L-tryptophan

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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