6nre
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Monomeric Lipocalin Can F 6== | |
+ | <StructureSection load='6nre' size='340' side='right'caption='[[6nre]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[6nre]] 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=6NRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NRE 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]] 2.06Å</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=6nre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nre OCA], [https://pdbe.org/6nre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nre RCSB], [https://www.ebi.ac.uk/pdbsum/6nre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nre ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/LI601_CANLF LI601_CANLF] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Lipocalins represent the most important protein family of the mammalian respiratory allergens. Four of the seven named dog allergens are lipocalins: Can f 1, Can f 2, Can f 4, and Can f 6. We present the structure of Can f 6 along with data on the biophysical and biological activity of this protein in comparison with other animal lipocalins. The Can f 6 structure displays the classic lipocalin calyx-shaped ligand binding cavity within a central beta-barrel similar to other lipocalins. Despite low sequence identity between the different dog lipocalin proteins, there is a high degree of structural similarity. On the other hand, Can f 6 has a similar primary sequence to cat, horse, mouse lipocalins as well as a structure that may underlie their cross reactivity. Interestingly, the entrance to the ligand binding pocket is capped by a His instead of the usually seen Tyr that may help select its natural ligand binding partner. Our highly pure recombinant Can f 6 is able to bind to human IgE (hIgE) demonstrating biological antigenicity. | ||
- | + | Structural characteristics of lipocalin allergens: Crystal structure of the immunogenic dog allergen Can f 6.,Clayton GM, White J, Lee S, Kappler JW, Chan SK PLoS One. 2019 Sep 16;14(9):e0213052. doi: 10.1371/journal.pone.0213052. , eCollection 2019. PMID:31525203<ref>PMID:31525203</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
+ | <div class="pdbe-citations 6nre" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Canis lupus familiaris]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Chan S]] | ||
+ | [[Category: Clayton G M]] | ||
+ | [[Category: Kappler J W]] |
Current revision
Monomeric Lipocalin Can F 6
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