1fmk: Difference between revisions
New page: left|200px<br /> <applet load="1fmk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fmk, resolution 1.5Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1fmk.gif|left|200px]]<br /> | [[Image:1fmk.gif|left|200px]]<br /><applet load="1fmk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1fmk" size=" | |||
caption="1fmk, resolution 1.5Å" /> | caption="1fmk, resolution 1.5Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of a large fragment of the c-Src tyrosine kinase, comprising | The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase. | ||
==Disease== | ==Disease== | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
1FMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http:// | 1FMK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMK OCA]. | ||
==Reference== | ==Reference== | ||
| Line 18: | Line 17: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
[[Category: Eck, M | [[Category: Eck, M J.]] | ||
[[Category: Harrison, S | [[Category: Harrison, S C.]] | ||
[[Category: Xu, W.]] | [[Category: Xu, W.]] | ||
[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| Line 30: | Line 29: | ||
[[Category: tyrosine kinase]] | [[Category: tyrosine kinase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:13 2008'' | ||
Revision as of 10:40, 21 February 2008
|
CRYSTAL STRUCTURE OF HUMAN TYROSINE-PROTEIN KINASE C-SRC
Overview
The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase.
Disease
Known disease associated with this structure: Colon cancer, advanced OMIM:[190090]
About this Structure
1FMK is a Single protein structure of sequence from Homo sapiens. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the tyrosine kinase c-Src., Xu W, Harrison SC, Eck MJ, Nature. 1997 Feb 13;385(6617):595-602. PMID:9024657
Page seeded by OCA on Thu Feb 21 12:40:13 2008
