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.


1f68

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f68.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1f68.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f68| PDB=1f68 | SCENE= }}
{{STRUCTURE_1f68| PDB=1f68 | SCENE= }}
-
'''NMR SOLUTION STRUCTURE OF THE BROMODOMAIN FROM HUMAN GCN5'''
+
===NMR SOLUTION STRUCTURE OF THE BROMODOMAIN FROM HUMAN GCN5===
-
==Overview==
+
<!--
-
The solution structure of the bromodomain from the human transcriptional coactivator GCN5 has been determined using NMR methods. The structure has a left-handed four-helix bundle topology, with two short additional helices in a long connecting loop. A hydrophobic groove and deep hydrophobic cavity are formed by loops at one end of the molecule. NMR binding experiments show that the cavity forms a specific binding pocket for the acetamide moiety. Peptides containing an N(epsilon)-acetylated lysine residue bind in this pocket with modest affinity (K(D) approximately 0.9 mM); no comparable binding occurs with unacetylated peptides. The GCN5 bromodomain binds the small ligands N(omega)-acetylhistamine and N-methylacetamide, confirming specificity for the alkyl acetamide moiety and showing that the primary element of recognition is simply the sterically unhindered terminal acetamide moiety of an acetylated lysine residue. Additional experiments show that binding is enhanced if the acetyl-lysine residue occurs within the context of a basic peptide and is inhibited by the presence of nearby acidic residues and by the carboxyl group of the free acetyl-lysine amino acid. The binding of the GCN5 bromodomain to acetylated peptides appears to have little additional sequence dependence, although weak interactions with other regions of the peptide are implicated by the binding data. Discrimination between ligands of positive and negative charge is attributed to the presence of several acidic residues located on the loops that form the sides of the binding pocket. Unlike the residues forming the acetamide binding cavity, these acidic side-chains are not conserved in other bromodomain sequences, suggesting that bromodomains might display differences in substrate selectivity and specificity as well as differences in function in vivo.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11090279}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11090279 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11090279}}
==About this Structure==
==About this Structure==
-
1F68 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=1F68 OCA].
+
1F68 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=1F68 OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Wright, P E.]]
[[Category: Wright, P E.]]
[[Category: Left-handed four-helix bundle]]
[[Category: Left-handed four-helix bundle]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:57:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:46:04 2008''

Revision as of 23:46, 30 June 2008

Image:1f68.png

Template:STRUCTURE 1f68

NMR SOLUTION STRUCTURE OF THE BROMODOMAIN FROM HUMAN GCN5

Template:ABSTRACT PUBMED 11090279

About this Structure

1F68 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain., Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE, J Mol Biol. 2000 Dec 1;304(3):355-70. PMID:11090279

Page seeded by OCA on Tue Jul 1 02:46:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f68"
Personal tools