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Biophysical studies of the allosteri...

Feng, Chao.

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Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs./
Author:	Feng, Chao.
Published:	Ann Arbor : ProQuest Dissertations & Theses, : 2016,
Description:	177 p.
Notes:	Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.
Contained By:	Dissertation Abstracts International78-02B(E).
Subject:	Biophysics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=10149324
ISBN:	9781369044423

Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs.
Feng, Chao.

Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs. - Ann Arbor : ProQuest Dissertations & Theses, 2016 - 177 p.

Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.

Thesis (Ph.D.)--Purdue University, 2016.

The non-receptor spleen tyrosine kinase (Syk) is an important player in signal transduction from immunoreceptors to various downstream targets. It is widely expressed in both haematopoietic and epithelial cells. Syk disorder is closely related with many inflammatory and autoimmune diseases, as well as cancers.

ISBN: 9781369044423Subjects--Topical Terms:

518360
Biophysics.

Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs.
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100 1 $a Feng, Chao. $3 2181502
245 1 0 $a Biophysical studies of the allosteric regulatory mechanism of Syk tandem SH2 domains interacting with immunoreceptor tyrosine-based activation motifs.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2016
300 $a 177 p.
500 $a Source: Dissertation Abstracts International, Volume: 78-02(E), Section: B.
500 $a Adviser: Carol B. Post.
502 $a Thesis (Ph.D.)--Purdue University, 2016.
520 $a The non-receptor spleen tyrosine kinase (Syk) is an important player in signal transduction from immunoreceptors to various downstream targets. It is widely expressed in both haematopoietic and epithelial cells. Syk disorder is closely related with many inflammatory and autoimmune diseases, as well as cancers.
520 $a Syk associates with immunoreceptors through its tandem SH2 domains (tSH2), which contain two SH2 domains connected by interdomain A. The association of Syk with immunoreceptors is regulated by Y130 phosphorylation in interdomain A. The unphosphorylated tSH2 can bind with the doubly phosphorylated immunoreceptor tyrosine-based activation motif (dp-ITAM) of the cytoplasmic domains of immunoreceptors with very high affinities (nanomolars for Kd). However, when Y130 is phosphorylated, the binding affinities drop drastically (micromolars for Kd). Interestingly, Y130 locates far (>20 A) from the binding sites and the detailed mechanism of this long-distance allosteric regulation is largely unknown.
520 $a A series of biophysical experiments, such as NMR and ITC, have been done to understand this allosteric mechanism. The results revealed interesting changes in the domain-domain coupling and multistate equilibrium thermodynamics of tSH2-ITAM interaction. These data suggested an entropic-allostery mechanism of Syk release from immunoreceptors. The new knowledge obtained from this work will help to explain the regulatory mechanism of Syk activity, assist the design for new drugs to treat Syk-related disorders, and promote researches of other kinases containing tandem SH2 domains.
590 $a School code: 0183.
650 4 $a Biophysics. $3 518360
650 4 $a Biochemistry. $3 518028
650 4 $a Bioinformatics. $3 553671
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710 2 $a Purdue University. $b Medicinal Chemistry and Molecular Pharmacology. $3 1285856
773 0 $t Dissertation Abstracts International $g 78-02B(E).
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793 $a English
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