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4ie3

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Revision as of 20:06, 5 August 2016

Crystal structure of human Arginase-2 complexed with inhbitor 1o

Structural highlights

4ie3 is a 3 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1d3v, 1pq3
Gene:	ARG2 (HUMAN)
Activity:	Arginase, with EC number 3.5.3.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ARGI2_HUMAN] May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, arginase II plays a role in both male and female sexual arousal. It is therefore a potential target for the treatment of male and female sexual arousal disorders.

Publication Abstract from PubMed

Substitution at the alpha center of the known human arginase inhibitor 2-amino-6-boronohexanoic acid (ABH) is acceptable in the active site pockets of both human arginase I and arginase II. In particular, substituents with a tertiary amine linked via a two carbon chain show improved inhibitory potency for both enzyme isoforms. This potency improvement can be rationalized by X-ray crystallography, which shows a water-mediated contact between the basic nitrogen and the carboxylic acid side chain of Asp200, which is situated at the mouth of the active site pocket of arginase II (Asp181 in arginase I). We believe that this is the first literature report of compounds with improved arginase inhibitory activity, relative to ABH, and represents a promising starting point for further optimization of in vitro potency and the identification of better tool molecules for in vivo investigations of the potential pathophysiological roles of arginases.

2-Substituted-2-amino-6-boronohexanoic acids as arginase inhibitors.,Golebiowski A, Paul Beckett R, Van Zandt M, Ji MK, Whitehouse D, Ryder TR, Jagdmann E, Andreoli M, Mazur A, Padmanilayam M, Cousido-Siah A, Mitschler A, Ruiz FX, Podjarny A, Schroeter H Bioorg Med Chem Lett. 2013 Apr 1;23(7):2027-30. doi: 10.1016/j.bmcl.2013.02.024. , Epub 2013 Feb 13. PMID:23453840^[1]

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

References

↑ Golebiowski A, Paul Beckett R, Van Zandt M, Ji MK, Whitehouse D, Ryder TR, Jagdmann E, Andreoli M, Mazur A, Padmanilayam M, Cousido-Siah A, Mitschler A, Ruiz FX, Podjarny A, Schroeter H. 2-Substituted-2-amino-6-boronohexanoic acids as arginase inhibitors. Bioorg Med Chem Lett. 2013 Apr 1;23(7):2027-30. doi: 10.1016/j.bmcl.2013.02.024. , Epub 2013 Feb 13. PMID:23453840 doi:http://dx.doi.org/10.1016/j.bmcl.2013.02.024

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ie3"

@@ Line 1: / Line 1: @@
 ==Crystal structure of human Arginase-2 complexed with inhbitor 1o==
 <StructureSection load='4ie3' size='340' side='right' caption='[[4ie3]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARG2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </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=4ie3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ie3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ie3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ie3 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=4ie3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ie3 OCA], [http://pdbe.org/4ie3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ie3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ie3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ie3 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4ie3" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Arginase|Arginase]]
 == References ==
 <references/>

4ie3

From Proteopedia

Revision as of 20:06, 5 August 2016

Crystal structure of human Arginase-2 complexed with inhbitor 1o

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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