3btn

<StructureSection load='3btn' size='340' side='right' caption='[[3btn]], [[Resolution|resolution]] 2.05&Aring;' scene=''>

<table><tr><td colspan='2'>[[3btn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BTN FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[7odc|7odc]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Azin1, Oazi, Oazin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</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=3btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3btn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3btn RCSB], [http://www.ebi.ac.uk/pdbsum/3btn PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bt/3btn_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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>

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[[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]]