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Pfam家族PF09410(DUF2006)首个代表成员的结构揭示了萼花蛋白超家族的一种结构特征,这表明其在脂质代谢中发挥作用。

Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.

作者信息

Chiu Hsiu Ju, Bakolitsa Constantina, Skerra Arne, Lomize Andrei, Carlton Dennis, Miller Mitchell D, Krishna S Sri, Abdubek Polat, Astakhova Tamara, Axelrod Herbert L, Clayton Thomas, Deller Marc C, Duan Lian, Feuerhelm Julie, Grant Joanna C, Grzechnik Slawomir K, Han Gye Won, Jaroszewski Lukasz, Jin Kevin K, Klock Heath E, Knuth Mark W, Kozbial Piotr, Kumar Abhinav, Marciano David, McMullan Daniel, Morse Andrew T, Nigoghossian Edward, Okach Linda, Paulsen Jessica, Reyes Ron, Rife Christopher L, van den Bedem Henry, Weekes Dana, Xu Qingping, Hodgson Keith O, Wooley John, Elsliger Marc André, Deacon Ashley M, Godzik Adam, Lesley Scott A, Wilson Ian A

机构信息

Joint Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1153-9. doi: 10.1107/S1744309109037749. Epub 2009 Dec 8.

DOI:10.1107/S1744309109037749
PMID:20944205
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2954199/
Abstract

The first structural representative of the domain of unknown function DUF2006 family, also known as Pfam family PF09410, comprises a lipocalin-like fold with domain duplication. The finding of the calycin signature in the N-terminal domain, combined with remote sequence similarity to two other protein families (PF07143 and PF08622) implicated in isoprenoid metabolism and the oxidative stress response, support an involvement in lipid metabolism. Clusters of conserved residues that interact with ligand mimetics suggest that the binding and regulation sites map to the N-terminal domain and to the interdomain interface, respectively.

摘要

未知功能结构域DUF2006家族(也称为Pfam家族PF09410)的首个结构代表,包含一个具有结构域重复的类脂质运载蛋白折叠结构。在N端结构域中发现的亲环素特征,再加上与参与类异戊二烯代谢和氧化应激反应的其他两个蛋白质家族(PF07143和PF08622)的远缘序列相似性,支持其参与脂质代谢。与配体模拟物相互作用的保守残基簇表明,结合位点和调节位点分别位于N端结构域和结构域间界面。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/e88f46bed39b/f-66-01153-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/a9c85abf1613/f-66-01153-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/7c977d220ecc/f-66-01153-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/e88f46bed39b/f-66-01153-fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/a9c85abf1613/f-66-01153-fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/7c977d220ecc/f-66-01153-fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f9b2/2954199/e88f46bed39b/f-66-01153-fig3.jpg

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