This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1stu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1stu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1stu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1stu| PDB=1stu | SCENE= }}
{{STRUCTURE_1stu| PDB=1stu | SCENE= }}
-
'''DOUBLE STRANDED RNA BINDING DOMAIN'''
+
===DOUBLE STRANDED RNA BINDING DOMAIN===
-
==Overview==
+
<!--
-
The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid motif that is found in a variety of proteins that interact with double-stranded (ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase, PKR. Drosophila staufen protein contains five copies of this motif, and the third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR methods, we have determined that staufen dsRBD3 forms a compact protein domain with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie on one face of a three-stranded anti-parallel beta-sheet. This structure is very similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5. Furthermore, the consensus derived from all known S5p family sequences shares several conserved residues with the dsRBD consensus sequence, indicating that the two domains share a common evolutionary origin. Using in vitro mutagenesis, we have identified several surface residues which are important for the RNA binding of the dsRBD, and these all lie on the same side of the domain. Two residues that are essential for RNA binding, F32 and K50, are also conserved in the S5 protein family, suggesting that the two domains interact with RNA in a similar way.
+
The line below this paragraph, {{ABSTRACT_PUBMED_7628456}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 7628456 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_7628456}}
==About this Structure==
==About this Structure==
-
1STU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STU OCA].
+
1STU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STU OCA].
==Reference==
==Reference==
Line 24: Line 28:
[[Category: Bycroft, M.]]
[[Category: Bycroft, M.]]
[[Category: Staufen]]
[[Category: Staufen]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:07:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:34:53 2008''

Revision as of 19:35, 28 July 2008

Image:1stu.png

Template:STRUCTURE 1stu

DOUBLE STRANDED RNA BINDING DOMAIN

Template:ABSTRACT PUBMED 7628456

About this Structure

1STU is a Single protein structure of sequence from Drosophila melanogaster. Full experimental information is available from OCA.

Reference

NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5., Bycroft M, Grunert S, Murzin AG, Proctor M, St Johnston D, EMBO J. 1995 Jul 17;14(14):3563-71. PMID:7628456

Page seeded by OCA on Mon Jul 28 22:34:53 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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