View source for 8ti5


==Crystal structure of Tyr p 36.0101==
<StructureSection load='8ti5' size='340' side='right'caption='[[8ti5]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ti5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tyrophagus_putrescentiae Tyrophagus putrescentiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TI5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TI5 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]] 1.15&#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=8ti5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ti5 OCA], [https://pdbe.org/8ti5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ti5 RCSB], [https://www.ebi.ac.uk/pdbsum/8ti5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ti5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1B2YLJ4_TYRPU A0A1B2YLJ4_TYRPU] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations.[RuleBase:RU003908]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural and allergenic characterization of mite profilins has not been previously pursued to a similar extent as plant profilins. Here, we describe structures of profilins originating from Tyrophagus putrescentiae (registered allergen Tyr p 36.0101) and Dermatophagoides pteronyssinus (here termed Der p profilin), which are the first structures of profilins from Arachnida. Additionally, the thermal stabilities of mite and plant profilins are compared, suggesting that the high number of cysteine residues in mite profilins may play a role in their increased stability. We also examine the cross-reactivity of plant and mite profilins as well as investigate the relevance of these profilins in mite inhalant allergy. Despite their high structural similarity to other profilins, mite profilins have low sequence identity with plant and human profilins. Subsequently, these mite profilins most likely do not display cross-reactivity with plant profilins. At the same time the profilins have highly conserved poly(l-proline) and actin binding sites.

Structural homology of mite profilins to plant profilins is not indicative of allergic cross-reactivity.,O'Malley A, Sankaran S, Carriuolo A, Khatri K, Kowal K, Chruszcz M Biol Chem. 2024 Apr 26. doi: 10.1515/hsz-2023-0366. PMID:38662449<ref>PMID:38662449</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ti5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tyrophagus putrescentiae]]
[[Category: Chruszcz M]]
[[Category: O'Malley A]]
[[Category: Sankaran S]]