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==1.6 A crystal structure of the lipocalin dog allergen Can f 1 with the C118S mutation==
<StructureSection load='8epu' size='340' side='right'caption='[[8epu]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8epu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EPU 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]] 1.6&#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=8epu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8epu OCA], [https://pdbe.org/8epu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8epu RCSB], [https://www.ebi.ac.uk/pdbsum/8epu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8epu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ALL1_CANLF ALL1_CANLF] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
INTRODUCTION: Pet lipocalins are respiratory allergens with a central hydrophobic ligand-binding cavity called a calyx. Molecules carried in the calyx by allergens are suggested to influence allergenicity, but little is known about the native ligands. METHODS: To provide more information on prospective ligands, we report crystal structures, NMR, molecular dynamics, and florescence studies of a dog lipocalin allergen Can f 1 and its closely related (and cross-reactive) cat allergen Fel d 7. RESULTS: Structural comparisons with reported lipocalins revealed that Can f 1 and Fel d 7 calyxes are open and positively charged while other dog lipocalin allergens are closed and negatively charged. We screened fatty acids as surrogate ligands, and found that Can f 1 and Fel d 7 bind multiple ligands with preferences for palmitic acid (16:0) among saturated fatty acids and oleic acid (18:1 cis-9) among unsaturated ones. NMR analysis of methyl probes reveals that conformational changes occur upon binding of pinolenic acid inside the calyx. Molecular dynamics simulation shows that the carboxylic group of fatty acids shuttles between two positively charged amino acids inside the Can f 1 and Fel d 7 calyx. Consistent with simulations, the stoichiometry of oleic acid-binding is 2:1 (fatty acid: protein) for Can f 1 and Fel d 7. DISCUSSION: The results provide valuable insights into the determinants of selectivity and candidate ligands for pet lipocalin allergens Can f 1 and Fel d 7.

Structural and ligand binding analysis of the pet allergens Can f 1 and Fel d 7.,Min J, Foo ACY, Gabel SA, Perera L, DeRose EF, Pomes A, Pedersen LC, Mueller GA Front Allergy. 2023 Mar 7;4:1133412. doi: 10.3389/falgy.2023.1133412. eCollection , 2023. PMID:36960093<ref>PMID:36960093</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8epu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canis lupus familiaris]]
[[Category: Large Structures]]
[[Category: Geoffrey MA]]
[[Category: Min J]]
[[Category: Pedersen LC]]