1awe

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1awe.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1awe.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1awe| PDB=1awe | SCENE= }}
{{STRUCTURE_1awe| PDB=1awe | SCENE= }}
-
'''HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES'''
+
===HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9374522}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9374522 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9374522}}
==About this Structure==
==About this Structure==
-
1AWE is a [[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].
+
1AWE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWE OCA].
==Reference==
==Reference==
Line 26: Line 30:
[[Category: Signal transduction]]
[[Category: Signal transduction]]
[[Category: So]]
[[Category: So]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:46:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:44:46 2008''

Revision as of 14:44, 30 June 2008

Image:1awe.png

Template:STRUCTURE 1awe

HUMAN SOS1 PLECKSTRIN HOMOLOGY (PH) DOMAIN, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9374522

About this Structure

1AWE is a Single protein structure of sequence from Homo sapiens. Full experimental 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 Mon Jun 30 17:44:46 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1awe"
Personal tools