5eqo: Difference between revisions

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'''Unreleased structure'''


The entry 5eqo is ON HOLD
==Human Angiogenin in complex with sulphate anions at an acidic solution==
<StructureSection load='5eqo' size='340' side='right'caption='[[5eqo]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5eqo]] 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=5EQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EQO 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5eqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eqo OCA], [https://pdbe.org/5eqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eqo RCSB], [https://www.ebi.ac.uk/pdbsum/5eqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eqo ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ANGI_HUMAN ANGI_HUMAN] Defects in ANG are the cause of susceptibility to amyotrophic lateral sclerosis type 9 (ALS9) [MIM:[https://omim.org/entry/611895 611895]. ALS is a degenerative disorder of motor neurons in the cortex, brain stem and spinal cord. ALS is characterized by muscular weakness and atrophy.<ref>PMID:17886298</ref> <ref>PMID:15557516</ref> <ref>PMID:16501576</ref> <ref>PMID:17900154</ref> <ref>PMID:18087731</ref> <ref>PMID:17703939</ref>
== Function ==
[https://www.uniprot.org/uniprot/ANGI_HUMAN ANGI_HUMAN] May function as a tRNA-specific ribonuclease that abolishes protein synthesis by specifically hydrolyzing cellular tRNAs. Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo.<ref>PMID:1400510</ref> <ref>PMID:19354288</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin (IC50 = 123.5 +/- 14.9 mm) is comparable to that previously reported for RNase A (119.0 +/- 6.5 mm) and RNase 2 (95.7 +/- 9.3 mm). However, analysis of two X-ray crystal structures of human angiogenin in complex with sulfate anions (in acidic and basic pH environments, respectively) indicates an entirely distinct mechanism of inhibition. While ammonium sulfate inhibits the ribonucleolytic activity of RNase A and RNase 2 by binding to the active site of these enzymes, sulfate anions bind only to peripheral substrate anion-binding subsites of human angiogenin, and not to the active site.


Authors: Chatzileontiadou, D.S.M., Leonidas, D.D.
The ammonium sulfate inhibition of human angiogenin.,Chatzileontiadou DS, Tsirkone VG, Dossi K, Kassouni AG, Liggri PG, Kantsadi AL, Stravodimos GA, Balatsos NA, Skamnaki VT, Leonidas DD FEBS Lett. 2016 Sep;590(17):3005-18. doi: 10.1002/1873-3468.12335. Epub 2016 Aug , 12. PMID:27483019<ref>PMID:27483019</ref>


Description: Human Angiogenin in complex with sulphate anions at an acidic solution
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Chatzileontiadou, D.S.M]]
<div class="pdbe-citations 5eqo" style="background-color:#fffaf0;"></div>
[[Category: Leonidas, D.D]]
 
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chatzileontiadou DSM]]
[[Category: Leonidas DD]]

Latest revision as of 11:17, 12 July 2023

Human Angiogenin in complex with sulphate anions at an acidic solutionHuman Angiogenin in complex with sulphate anions at an acidic solution

Structural highlights

5eqo is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ANGI_HUMAN Defects in ANG are the cause of susceptibility to amyotrophic lateral sclerosis type 9 (ALS9) [MIM:611895. ALS is a degenerative disorder of motor neurons in the cortex, brain stem and spinal cord. ALS is characterized by muscular weakness and atrophy.[1] [2] [3] [4] [5] [6]

Function

ANGI_HUMAN May function as a tRNA-specific ribonuclease that abolishes protein synthesis by specifically hydrolyzing cellular tRNAs. Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo.[7] [8]

Publication Abstract from PubMed

In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin (IC50 = 123.5 +/- 14.9 mm) is comparable to that previously reported for RNase A (119.0 +/- 6.5 mm) and RNase 2 (95.7 +/- 9.3 mm). However, analysis of two X-ray crystal structures of human angiogenin in complex with sulfate anions (in acidic and basic pH environments, respectively) indicates an entirely distinct mechanism of inhibition. While ammonium sulfate inhibits the ribonucleolytic activity of RNase A and RNase 2 by binding to the active site of these enzymes, sulfate anions bind only to peripheral substrate anion-binding subsites of human angiogenin, and not to the active site.

The ammonium sulfate inhibition of human angiogenin.,Chatzileontiadou DS, Tsirkone VG, Dossi K, Kassouni AG, Liggri PG, Kantsadi AL, Stravodimos GA, Balatsos NA, Skamnaki VT, Leonidas DD FEBS Lett. 2016 Sep;590(17):3005-18. doi: 10.1002/1873-3468.12335. Epub 2016 Aug , 12. PMID:27483019[9]

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

See Also

References

  1. ↑ Wu D, Yu W, Kishikawa H, Folkerth RD, Iafrate AJ, Shen Y, Xin W, Sims K, Hu GF. Angiogenin loss-of-function mutations in amyotrophic lateral sclerosis. Ann Neurol. 2007 Dec;62(6):609-17. PMID:17886298 doi:10.1002/ana.21221
  2. ↑ Greenway MJ, Alexander MD, Ennis S, Traynor BJ, Corr B, Frost E, Green A, Hardiman O. A novel candidate region for ALS on chromosome 14q11.2. Neurology. 2004 Nov 23;63(10):1936-8. PMID:15557516
  3. ↑ Greenway MJ, Andersen PM, Russ C, Ennis S, Cashman S, Donaghy C, Patterson V, Swingler R, Kieran D, Prehn J, Morrison KE, Green A, Acharya KR, Brown RH Jr, Hardiman O. ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis. Nat Genet. 2006 Apr;38(4):411-3. Epub 2006 Feb 26. PMID:16501576 doi:10.1038/ng1742
  4. ↑ Crabtree B, Thiyagarajan N, Prior SH, Wilson P, Iyer S, Ferns T, Shapiro R, Brew K, Subramanian V, Acharya KR. Characterization of human angiogenin variants implicated in amyotrophic lateral sclerosis. Biochemistry. 2007 Oct 23;46(42):11810-8. Epub 2007 Sep 27. PMID:17900154 doi:10.1021/bi701333h
  5. ↑ Gellera C, Colombrita C, Ticozzi N, Castellotti B, Bragato C, Ratti A, Taroni F, Silani V. Identification of new ANG gene mutations in a large cohort of Italian patients with amyotrophic lateral sclerosis. Neurogenetics. 2008 Feb;9(1):33-40. Epub 2007 Dec 18. PMID:18087731 doi:10.1007/s10048-007-0111-3
  6. ↑ Conforti FL, Sprovieri T, Mazzei R, Ungaro C, La Bella V, Tessitore A, Patitucci A, Magariello A, Gabriele AL, Tedeschi G, Simone IL, Majorana G, Valentino P, Condino F, Bono F, Monsurro MR, Muglia M, Quattrone A. A novel Angiogenin gene mutation in a sporadic patient with amyotrophic lateral sclerosis from southern Italy. Neuromuscul Disord. 2008 Jan;18(1):68-70. Epub 2007 Aug 20. PMID:17703939 doi:S0960-8966(07)00676-1
  7. ↑ Saxena SK, Rybak SM, Davey RT Jr, Youle RJ, Ackerman EJ. Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. J Biol Chem. 1992 Oct 25;267(30):21982-6. PMID:1400510
  8. ↑ Dickson KA, Kang DK, Kwon YS, Kim JC, Leland PA, Kim BM, Chang SI, Raines RT. Ribonuclease inhibitor regulates neovascularization by human angiogenin. Biochemistry. 2009 May 12;48(18):3804-6. doi: 10.1021/bi9005094. PMID:19354288 doi:10.1021/bi9005094
  9. ↑ Chatzileontiadou DS, Tsirkone VG, Dossi K, Kassouni AG, Liggri PG, Kantsadi AL, Stravodimos GA, Balatsos NA, Skamnaki VT, Leonidas DD. The ammonium sulfate inhibition of human angiogenin. FEBS Lett. 2016 Sep;590(17):3005-18. doi: 10.1002/1873-3468.12335. Epub 2016 Aug , 12. PMID:27483019 doi:http://dx.doi.org/10.1002/1873-3468.12335

5eqo, resolution 2.40Å

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