東華大學圖書館 |

語系: 繁體中文

說明(常見問題)

回圖書館首頁

手機版館藏查詢

登入

回首頁

切換: 標籤 | MARC模式 | ISBD

Structural and functional characteri...

Nolen, Bradley James.

FindBook

Google Book

Amazon

博客來

Structural and functional characterization of Sky1p, an SR protein kinase in yeast.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structural and functional characterization of Sky1p, an SR protein kinase in yeast./
作者:	Nolen, Bradley James.
面頁冊數:	170 p.
附註:	Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.
Contained By:	Dissertation Abstracts International64-08B.
標題:	Chemistry, Biochemistry. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3100374
ISBN:	0496479657

Structural and functional characterization of Sky1p, an SR protein kinase in yeast.
Nolen, Bradley James.

Structural and functional characterization of Sky1p, an SR protein kinase in yeast. - 170 p.

Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.

Thesis (Ph.D.)--University of California, San Diego, 2003.

The SR protein kinases (SRPKs) are constitutively active serine kinases with important roles in RNA processing, ion homeostasis, and drug sensitivity. Through a combination of X-ray crystallographic and biochemical methods, I have investigated the regulation, substrate specificity and catalytic mechanism of Sky1p, an SRPK from Saccharomyces cerevisiae.

ISBN: 0496479657Subjects--Topical Terms:

1017722
Chemistry, Biochemistry.

Structural and functional characterization of Sky1p, an SR protein kinase in yeast.
LDR:03278nmm 2200313 4500 001 1837504
005 20050506072707.5
008 130614s2003 eng d
020 $a 0496479657
035 $a (UnM)AAI3100374
035 $a AAI3100374
040 $a UnM $c UnM
100 1 $a Nolen, Bradley James. $3 1925950
245 1 0 $a Structural and functional characterization of Sky1p, an SR protein kinase in yeast.
300 $a 170 p.
500 $a Source: Dissertation Abstracts International, Volume: 64-08, Section: B, page: 3809.
500 $a Chair: Gourisankar Ghosh.
502 $a Thesis (Ph.D.)--University of California, San Diego, 2003.
520 $a The SR protein kinases (SRPKs) are constitutively active serine kinases with important roles in RNA processing, ion homeostasis, and drug sensitivity. Through a combination of X-ray crystallographic and biochemical methods, I have investigated the regulation, substrate specificity and catalytic mechanism of Sky1p, an SRPK from Saccharomyces cerevisiae.
520 $a Sky1p and the other SRPKs are unusual in that they are constitutively active, i.e., their activity is not dependent on activation loop phosphorylation or interaction with regulatory factors. I have determined the molecular basis for the constitutive activity of Sky1p. While the activation loop changes conformation in response to phosphorylation in other kinases, it is locked into the active conformation in Sky1p. This is accomplished through the action of the C-terminal tail, which braces one end of the loop, and an SRPK-conserved glutamine that pins down the other end. Our studies have also revealed an insert unique to SRPKs that may be involved in positioning helix alphaC for activity and an anion binding pocket in the small lobe that may be important for Sky1p activity in vivo.
520 $a The SRPKs phosphorylate serines embedded in stretches of consecutive serine-arginine repeats. Our studies have established that a negatively charged residue in the substrate is critical for recognition. The crystal structure of Sky1p shows how this residue and the arginines that surround it are recognized by SRPKs. Together, these results support a sequential mechanism for phosphorylation of RS repeats by SRPKs in which a previously phosphorylated serine becomes a recognition element for later rounds of phosphorylation.
520 $a Conformational changes are thought to play a key role in the catalytic cycle of active protein kinases, but little is known about the atomic details of these changes and how they relate to the catalytic mechanism. We have determined the structures of Sky1p in four different states of nucleotide binding. By comparing the apoenzyme structure to the ADP and ATP-bound Sky1p structures, we have revealed conformational changes caused by ATP binding or conversion from nucleotide reactant to product. The structure of a bound ATP analogue revealed specific interactions at the active site that are required for nucleotide-induced conformational changes.
590 $a School code: 0033.
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Biophysics, General. $3 1019105
690 $a 0487
690 $a 0786
710 2 0 $a University of California, San Diego. $3 1018093
773 0 $t Dissertation Abstracts International $g 64-08B.
790 1 0 $a Ghosh, Gourisankar, $e advisor
790 $a 0033
791 $a Ph.D.
792 $a 2003
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3100374