View source for 4peq


==Structure of bovine ribonuclease inhibitor complexed with bovine ribonuclease I==
<StructureSection load='4peq' size='340' side='right'caption='[[4peq]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4peq]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PEQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PEQ 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]] 2.211&#8491;</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=4peq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4peq OCA], [https://pdbe.org/4peq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4peq RCSB], [https://www.ebi.ac.uk/pdbsum/4peq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4peq 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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease inhibitor (RI) is a conserved protein of the mammalian cytosol. RI binds with high affinity to diverse secretory ribonucleases (RNases) and inhibits their enzymatic activity. Although secretory RNases are found in all vertebrates, the existence of a non-mammalian RI has been uncertain. Here, we report on the identification and characterization of RI homologs from chicken and anole lizard. These proteins bind to RNases from multiple species, but exhibit much greater affinity for their cognate RNases than for mammalian RNases. To reveal the basis for this differential affinity, we determined the crystal structure of mouse, bovine, and chicken RI.RNase complexes to a resolution of 2.20, 2.21, and 1.92A, respectively. A combination of structural, computational, and bioinformatic analyses enabled the identification of two residues that appear to contribute to the differential affinity for RNases. We also found marked differences in oxidative instability between mammalian and non-mammalian RIs, indicating evolution toward greater oxygen-sensitivity in RIs from mammalian species. Taken together, our results illuminate the structural and functional evolution of RI, along with its dynamic role in vertebrate biology.

Functional Evolution of Ribonuclease Inhibitor: Insights from Birds and Reptiles.,Lomax JE, Bianchetti CM, Chang A, Phillips GN Jr, Fox BG, Raines RT J Mol Biol. 2014 Jun 15. pii: S0022-2836(14)00287-3. doi:, 10.1016/j.jmb.2014.06.007. PMID:24941155<ref>PMID:24941155</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4peq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
*[[Ribonuclease inhibitor|Ribonuclease inhibitor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Bianchetti CM]]
[[Category: Fox BG]]
[[Category: Lomax JE]]
[[Category: Raines RT]]