1gv7: Difference between revisions

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[[Image:1gv7.gif|left|200px]]
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{{STRUCTURE_1gv7|  PDB=1gv7  |  SCENE=  }}
'''ARH-I, AN ANGIOGENIN/RNASE A CHIMERA'''


==ARH-I, an angiogenin/RNase A chimera==
<StructureSection load='1gv7' size='340' side='right'caption='[[1gv7]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gv7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GV7 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1gv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gv7 OCA], [https://pdbe.org/1gv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gv7 RCSB], [https://www.ebi.ac.uk/pdbsum/1gv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gv7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</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/gv/1gv7_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=1gv7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Angiogenin and ribonuclease A share 33% sequence identity but have distinct functions. Angiogenin is a potent inducer of angiogenesis that is only weakly ribonucleolytic, whereas ribonuclease A is a robust ribonuclease that is not angiogenic. A chimera ("ARH-I"), in which angiogenin residues 58-70 are replaced with residues 59-73 of ribonuclease A, has intermediate ribonucleolytic potency and no angiogenic activity. Here we report a crystal structure of ARH-I that reveals the molecular basis for these characteristics. The ribonuclease A-derived (guest) segment adopts a structure largely similar to that in ribonuclease A, and successfully converts this region from a cell-binding site to a purine-binding site. At the same time, its presence causes complex changes in the angiogenin-derived (host) portion that account for much of the increased ribonuclease activity of ARH-I. Guest-host interactions of this type probably occur more generally in protein chimeras, emphasizing the importance of direct structural information for understanding the functional behavior of such molecules.


==Overview==
Guest-host crosstalk in an angiogenin-RNase A chimeric protein.,Holloway DE, Shapiro R, Hares MC, Leonidas DD, Acharya KR Biochemistry. 2002 Aug 20;41(33):10482-9. PMID:12173935<ref>PMID:12173935</ref>
Angiogenin and ribonuclease A share 33% sequence identity but have distinct functions. Angiogenin is a potent inducer of angiogenesis that is only weakly ribonucleolytic, whereas ribonuclease A is a robust ribonuclease that is not angiogenic. A chimera ("ARH-I"), in which angiogenin residues 58-70 are replaced with residues 59-73 of ribonuclease A, has intermediate ribonucleolytic potency and no angiogenic activity. Here we report a crystal structure of ARH-I that reveals the molecular basis for these characteristics. The ribonuclease A-derived (guest) segment adopts a structure largely similar to that in ribonuclease A, and successfully converts this region from a cell-binding site to a purine-binding site. At the same time, its presence causes complex changes in the angiogenin-derived (host) portion that account for much of the increased ribonuclease activity of ARH-I. Guest-host interactions of this type probably occur more generally in protein chimeras, emphasizing the importance of direct structural information for understanding the functional behavior of such molecules.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1GV7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens,_bos_taurus Homo sapiens, bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GV7 OCA].
</div>
<div class="pdbe-citations 1gv7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Guest-host crosstalk in an angiogenin-RNase A chimeric protein., Holloway DE, Shapiro R, Hares MC, Leonidas DD, Acharya KR, Biochemistry. 2002 Aug 20;41(33):10482-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12173935 12173935]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
[[Category: Homo sapiens, bos taurus]]
== References ==
[[Category: Pancreatic ribonuclease]]
<references/>
[[Category: Single protein]]
__TOC__
[[Category: Acharya, K R.]]
</StructureSection>
[[Category: Hares, M C.]]
[[Category: Bos taurus]]
[[Category: Holloway, D E.]]
[[Category: Homo sapiens]]
[[Category: Leonidas, D D.]]
[[Category: Large Structures]]
[[Category: Shapiro, R.]]
[[Category: Acharya KR]]
[[Category: Angiogenesis]]
[[Category: Hares MC]]
[[Category: Angiogenin]]
[[Category: Holloway DE]]
[[Category: Chimera]]
[[Category: Leonidas DD]]
[[Category: Homolog scanning mutagenesis]]
[[Category: Shapiro R]]
[[Category: Hybrid]]
[[Category: Pancreatic ribonuclease]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:03:03 2008''

Latest revision as of 11:28, 6 November 2024

ARH-I, an angiogenin/RNase A chimeraARH-I, an angiogenin/RNase A chimera

Structural highlights

1gv7 is a 1 chain structure with sequence from Bos taurus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNAS1_BOVIN Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Angiogenin and ribonuclease A share 33% sequence identity but have distinct functions. Angiogenin is a potent inducer of angiogenesis that is only weakly ribonucleolytic, whereas ribonuclease A is a robust ribonuclease that is not angiogenic. A chimera ("ARH-I"), in which angiogenin residues 58-70 are replaced with residues 59-73 of ribonuclease A, has intermediate ribonucleolytic potency and no angiogenic activity. Here we report a crystal structure of ARH-I that reveals the molecular basis for these characteristics. The ribonuclease A-derived (guest) segment adopts a structure largely similar to that in ribonuclease A, and successfully converts this region from a cell-binding site to a purine-binding site. At the same time, its presence causes complex changes in the angiogenin-derived (host) portion that account for much of the increased ribonuclease activity of ARH-I. Guest-host interactions of this type probably occur more generally in protein chimeras, emphasizing the importance of direct structural information for understanding the functional behavior of such molecules.

Guest-host crosstalk in an angiogenin-RNase A chimeric protein.,Holloway DE, Shapiro R, Hares MC, Leonidas DD, Acharya KR Biochemistry. 2002 Aug 20;41(33):10482-9. PMID:12173935[2]

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

See Also

References

  1. ↑ delCardayre SB, Ribo M, Yokel EM, Quirk DJ, Rutter WJ, Raines RT. Engineering ribonuclease A: production, purification and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 1995 Mar;8(3):261-73. PMID:7479688
  2. ↑ Holloway DE, Shapiro R, Hares MC, Leonidas DD, Acharya KR. Guest-host crosstalk in an angiogenin-RNase A chimeric protein. Biochemistry. 2002 Aug 20;41(33):10482-9. PMID:12173935

1gv7, resolution 2.10Å

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