1ysm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ysm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ysm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ysm| PDB=1ysm | SCENE= }}
{{STRUCTURE_1ysm| PDB=1ysm | SCENE= }}
-
'''NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.'''
+
===NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.===
-
==Overview==
+
<!--
-
Siah-interacting protein (SIP) was identified as a novel adaptor that physically links the E3 ubiquitin ligase activity of Siah-1 with Skp1 and Ebi F-Box protein in the degradation of beta-catenin, a transcriptional activator of TCF/LEF genes. In this study, we have used solution NMR spectroscopy to characterize the domain structure of SIP, which includes a novel helical hairpin domain at the N-terminus flexibly linked to a CS domain and an unstructured carboxy terminal SGS domain. These studies have been complemented by mapping the sites of functionally important protein-protein interactions involving Siah-1 and Skp1 to individual domains of SIP. NMR-based chemical shift perturbation assays show that Siah-1 interacts with the flexible linker between SIP N and CS domains. This site for interaction in the linker does not perturb residues in the structured region at the N-terminus but does appear to restrict the rotational freedom of the SIP CS domain in the context of the full-length protein. In contrast, Skp1 engages the SIP CS domain exclusively through weak interactions that are not coupled to the other domains. The principal role of the modular structure of SIP appears to be in bringing these two proteins into physical proximity and orchestrating the orientation required for polyubiquitination of beta-catenin in the intact SCF-type complex.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15996101}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15996101 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15996101}}
==About this Structure==
==About this Structure==
-
1YSM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSM OCA].
+
1YSM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSM OCA].
==Reference==
==Reference==
Line 30: Line 34:
[[Category: Michowski, W.]]
[[Category: Michowski, W.]]
[[Category: Helix-turn-helix]]
[[Category: Helix-turn-helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:43:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:20:44 2008''

Revision as of 17:20, 27 July 2008

Image:1ysm.png

Template:STRUCTURE 1ysm

NMR Structure of N-terminal domain (Residues 1-77) of Siah-Interacting Protein.

Template:ABSTRACT PUBMED 15996101

About this Structure

1YSM is a Single protein structure of sequence from Mus musculus. Full experimental information is available from OCA.

Reference

The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies., Bhattacharya S, Lee YT, Michowski W, Jastrzebska B, Filipek A, Kuznicki J, Chazin WJ, Biochemistry. 2005 Jul 12;44(27):9462-71. PMID:15996101

Page seeded by OCA on Sun Jul 27 20:20:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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