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.


1b64

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1b64" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b64" /> '''SOLUTION STRUCTURE OF THE GUANINE NUCLEOTID...)
Line 8: Line 8:
==About this Structure==
==About this Structure==
-
1B64 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA]].
+
1B64 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Structure known Active Site: GEF. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B64 OCA]].
==Reference==
==Reference==
Line 25: Line 25:
[[Category: translation elongation]]
[[Category: translation elongation]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:10:03 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:30:21 2007''

Revision as of 06:25, 30 October 2007


1b64

Drag the structure with the mouse to rotate

SOLUTION STRUCTURE OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR DOMAIN FROM HUMAN ELONGATION FACTOR-ONE BETA, NMR, 20 STRUCTURES

Overview

BACKGROUND: In eukaryotic protein synthesis, the multi-subunit elongation, factor 1 (EF-1) plays an important role in ensuring the fidelity and, regulating the rate of translation. EF-1alpha, which transports the, aminoacyl tRNA to the ribosome, is a member of the G-protein superfamily., EF-1beta regulates the activity of EF-1alpha by catalyzing the exchange of, GDP for GTP and thereby regenerating the active form of EF-1alpha. The, structure of the bacterial analog of EF-1alpha, EF-Tu has been solved in, complex with its GDP exchange factor, EF-Ts. These structures indicate a, mechanism for GDP-GTP exchange in prokaryotes. Although there is good, sequence conservation between EF-1alpha and EF-Tu, there is essentially no, sequence similarity between EF-1beta and EF-Ts. We wished to ... [(full description)]

About this Structure

1B64 is a [Single protein] structure of sequence from [Homo sapiens]. Structure known Active Site: GEF. Full crystallographic information is available from [OCA].

Reference

The solution structure of the guanine nucleotide exchange domain of human elongation factor 1beta reveals a striking resemblance to that of EF-Ts from Escherichia coli., Perez JM, Siegal G, Kriek J, Hard K, Dijk J, Canters GW, Moller W, Structure. 1999 Feb 15;7(2):217-26. PMID:10368288

Page seeded by OCA on Tue Oct 30 08:30:21 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools