1awe
From Proteopedia
(New page: 200px<br /> <applet load="1awe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1awe" /> '''HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN,...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1awe. | + | [[Image:1awe.jpg|left|200px]]<br /><applet load="1awe" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1awe" size=" | + | |
caption="1awe" /> | caption="1awe" /> | ||
'''HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES'''<br /> | '''HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1AWE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1AWE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWE OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 22: | ||
[[Category: sos]] | [[Category: sos]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:30:00 2008'' |
Revision as of 13:30, 15 February 2008
|
HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES
Contents |
Overview
A large subset of pleckstrin homology (PH) domains are immediately to the, C terminus of diffuse B cell lymphoma (Dbl) homology (DbH) domains. Dbl, domains are generally considered to be GTPase-exchange factors; many are, proto-oncogenes. PH domains appear to function as membrane-recruitment, factors, or have specific protein-protein interactions. Since dual domain, (DbH/PH) constructs are known to have significant properties in other, pathways, it is possible that a defined interdomain relationship is, required for DbH/PH function. We determined the solution structure of the, human SOS1 PH domain for a construct partially extended into the preceding, DbH domain. There are specific structural contacts between the PH and the, vestigial DbH domain. This appears to involve structural elements common, to this subfamily of PH domains, and to DbH domains. The human SOS1 PH, domain binds to inositol 1,4,5-triphosphate with a approximately 60 mu M, affinity. Using chemical shift titration, the binding site is identified, to be essentially identical to that observed crystallographically for the, inositol 1,4,5-triphosphate complex with the PH domain of phospholipase, Cdelta. This site may serve as an interdomain regulator of DbH or other, domains' functions. While the overall fold of the human SOS1 PH domain is, similar to other PH domains, the size and position of the intrastrand, loops and the presence of an N-terminal alpha-helix of the vestigial DbH, domain suggest that the subfamily of PH domains associated with DbH, domains may be a well defined structural group in which the PH domain is a, membrane recruiter and modulator.
Disease
Known diseases associated with this structure: Fibromatosis, gingival OMIM:[182530], Noonan syndrome 4 OMIM:[182530]
About this Structure
1AWE is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The solution structure of the pleckstrin homology domain of human SOS1. A possible structural role for the sequential association of diffuse B cell lymphoma and pleckstrin homology domains., Zheng J, Chen RH, Corblan-Garcia S, Cahill SM, Bar-Sagi D, Cowburn D, J Biol Chem. 1997 Nov 28;272(48):30340-4. PMID:9374522
Page seeded by OCA on Fri Feb 15 15:30:00 2008
