View source for 9cqg


==CRYSTAL STRUCTURE OF APO C-TERMINAL HIS-TAG DOG HSP47(36-418) IN A P 1 CRYSTAL FORM==
<StructureSection load='9cqg' size='340' side='right'caption='[[9cqg]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cqg]] is a 8 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=9CQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CQG 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]] 2.474&#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=9cqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cqg OCA], [https://pdbe.org/9cqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cqg RCSB], [https://www.ebi.ac.uk/pdbsum/9cqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cqg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C7C419_CANLF C7C419_CANLF] Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.[ARBA:ARBA00025405]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Heat-shock protein 47 (HSP47) is a potential target for inhibitors that ameliorate fibrosis by reducing collagen assembly. In an effort to develop a structure-based drug-design system, it was not possible to replicate a previous literature result (PDB entry 4au4) for apo dog HSP47; instead, crystal forms were obtained in which pairs of dog HSP47 molecules interacted through a noncleavable C-terminal His-tag to build up tetramers, all of which had multiple molecules of HSP47 in the asymmetric unit and none of which diffracted as well as the literature precedent. To overcome these difficulties, a two-pronged approach was followed: (i) the His-tag was moved from the C-terminus to the N-terminus and was made cleavable, and (ii) Adnectin (derived from the tenth domain of human fibronectin type III) crystallization chaperones were developed. Both approaches provided well diffracting crystals, but the latter approach yielded crystal forms with only one or two HSP47 complexes per asymmetric unit, which made model building less onerous.

Improving the diffraction quality of heat-shock protein 47 crystals.,Kish K, Cobell S, Szapiel N, Yan C, Newitt JA, Tredup J, Rodrigo I, Tomasco E, Gao M, Marsilio F, Haugner J, Lipovsek D, Deng B, Bousquet P, Zhang Y, Schmidt H, Sheriff S Acta Crystallogr F Struct Biol Commun. 2024 Nov 1. doi: , 10.1107/S2053230X24009233. PMID:39397789<ref>PMID:39397789</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cqg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Canis lupus familiaris]]
[[Category: Large Structures]]
[[Category: Sheriff S]]