1x9x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1x9x.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1x9x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1x9x| PDB=1x9x | SCENE= }}
{{STRUCTURE_1x9x| PDB=1x9x | SCENE= }}
-
'''Solution Structure of Dimeric SAM Domain from MAPKKK Ste11'''
+
===Solution Structure of Dimeric SAM Domain from MAPKKK Ste11===
-
==Overview==
+
<!--
-
Ste11, a homologue of mammalian MAPKKKs, together with its binding partner Ste50 works in a number of MAPK signaling pathways of Saccharomyces cerevisiae. Ste11/Ste50 binding is mediated by their sterile alpha motifs or SAM domains, of which homologues are also found in many other intracellular signaling and regulatory proteins. Here, we present the solution structure of the SAM domain or residues D37-R104 of Ste11 and its interactions with the cognate SAM domain-containing region of Ste50, residues M27-Q131. NMR pulse-field-gradient (PFG) and rotational correlation time measurements (tauc) establish that the Ste11 SAM domain exists predominantly as a symmetric dimer in solution. The solution structure of the dimeric Ste11 SAM domain consists of five well-defined helices per monomer packed into a compact globular structure. The dimeric structure of the SAM domain is maintained by a novel dimer interface involving interactions between a number of hydrophobic residues situated on helix 4 and at the beginning of the C-terminal long helix (helix 5). The dimer structure may also be stabilized by potential salt bridge interactions across the interface. NMR H/2H exchange experiments showed that binding of the Ste50 SAM to the Ste11 SAM very likely involves the positively charged extreme C-terminal region as well as exposed hydrophobic patches of the dimeric Ste11 SAM domain. The dimeric structure of the Ste11 SAM and its interactions with the Ste50 SAM may have important roles in the regulation and activation of the Ste11 kinase and signal transmission and amplifications through the Ste50-Ste11 complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15544813}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15544813 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15544813}}
==About this Structure==
==About this Structure==
-
1X9X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9X OCA].
+
1X9X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X9X OCA].
==Reference==
==Reference==
Line 33: Line 37:
[[Category: Sam domain]]
[[Category: Sam domain]]
[[Category: Ste11]]
[[Category: Ste11]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:45:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:31:23 2008''

Revision as of 05:31, 29 July 2008

Image:1x9x.png

Template:STRUCTURE 1x9x

Solution Structure of Dimeric SAM Domain from MAPKKK Ste11

Template:ABSTRACT PUBMED 15544813

About this Structure

1X9X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

Reference

Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex., Bhattacharjya S, Xu P, Gingras R, Shaykhutdinov R, Wu C, Whiteway M, Ni F, J Mol Biol. 2004 Dec 3;344(4):1071-87. PMID:15544813

Page seeded by OCA on Tue Jul 29 08:31:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1x9x"
Personal tools