Structural characterization of recombinant human fibroblast growth factor receptor 2b kinase domain upon interaction with omega fatty acids

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• 作者：Masoumeh Moghadasi^a ; ¹ ; Dariush Ilghari^b ; ¹ ; Majid Sirati-Sabet^c ; Abbas Amini^d ; ^e ; ^{a.amini@westernsydney.edu.au} ; ^{a.amini@ack.edu.kw} ; Hamideh Asghari^a ; Nematollah Gheibi^f ; ^{ngheibi@qums.ac.ir}
• 关键词：hFGFR2b ; human fibroblast growth factor receptor 2b ; UFAs ; unsaturated fatty acids ; CD ; circular dichroism ; FGFRs ; fibroblast growth factor receptors ; RTK ; receptor tyrosine kinase ; Ig ; immunoglobulin ; PLCγ ; phospholipase Cγ ; FRS2 ; fibroblast growth factor substrate 2 ; AS ; apert syndrome ; LADD ; Lacrimo-Auriculo-Dento-Digital Syndrome ; OA ; oleic acid ; LA ; linoleic acid ; ALA ; α-linolenic acid ; EtOH ; ethanol ; IPTG ; isopropyl -d-1-thiogalactopyranoside &minus ; PLCG1 ; phospholipase C ; gamma 1 ; Trp ; t
• 刊名：Chemistry and Physics of Lipids
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：202
• 期：Complete
• 页码：21-27
• 全文大小：1283 K
• 卷排序：202

文摘

Mutations within the tyrosine kinase domain lead to an activation of hFGFR2b. PUFAs interact with hFGFR2b KD and alter the position of hydrophobic residues. Changes in hFGFR2b and interacting with UFAs modify the signal transduction process. UFAs change the tertiary structure of hFGFR2b KD not its secondary structure.