3btn

<table><tr><td colspan='2'>[[3btn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BTN FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7odc|7odc]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Azin1, Oazi, Oazin ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>

[[https://www.uniprot.org/uniprot/AZIN1_MOUSE AZIN1_MOUSE]] Inhibits antizyme-dependent ODC degradation by binding to antizyme with greater affinity. Regulates cellular polyamine homeostasis.<ref>PMID:10698696</ref> <ref>PMID:18369191</ref>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Antizyme inhibitor (AzI) regulates cellular polyamine homeostasis by binding to the polyamine-induced protein, Antizyme (Az), with greater affinity than ornithine decarboxylase (ODC). AzI is highly homologous to ODC but is not enzymatically active. In order to understand these specific characteristics of AzI and its differences from ODC, we determined the 3D structure of mouse AzI to 2.05 A resolution. Both AzI and ODC crystallize as a dimer. However, fewer interactions at the dimer interface, a smaller buried surface area, and lack of symmetry of the interactions between residues from the two monomers in the AzI structure suggest that this dimeric structure is nonphysiological. In addition, the absence of residues and interactions required for pyridoxal 5'-phosphate (PLP) binding suggests that AzI does not bind PLP. Biochemical studies confirmed the lack of PLP binding and revealed that AzI exists as a monomer in solution while ODC is dimeric. Our findings that AzI exists as a monomer and is unable to bind PLP provide two independent explanations for its lack of enzymatic activity and suggest the basis for its enhanced affinity toward Az.

Crystallographic and biochemical studies revealing the structural basis for antizyme inhibitor function.,Albeck S, Dym O, Unger T, Snapir Z, Bercovich Z, Kahana C Protein Sci. 2008 May;17(5):793-802. Epub 2008 Mar 27. PMID:18369191<ref>PMID:18369191</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3btn" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Albeck, S]]

[[Category: Dym, O]]

[[Category: ISPC, Israel Structural Proteomics Center]]

[[Category: Kahana, C]]

[[Category: Unger, T]]

[[Category: Tim-like a/b barrel domain and a sheet domain]]