2rnx: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Newer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px <!-- The line below this paragraph, containing "STRUCTURE_2rnx", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2rnx.jpg|left|200px]]
{{Seed}}
[[Image:2rnx.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rnx|  PDB=2rnx  |  SCENE=  }}  
{{STRUCTURE_2rnx|  PDB=2rnx  |  SCENE=  }}  


'''The Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the Bromodomains of the HUman Transcriptional Co-Activators PCAF and CBP'''
===The Structural Basis for Site-Specific Lysine-Acetylated Histone Recognition by the Bromodomains of the HUman Transcriptional Co-Activators PCAF and CBP===




==Overview==
<!--
Histone lysine acetylation is central to epigenetic control of gene transcription. Bromodomains of chromosomal proteins function as acetyl-lysine (Kac) binding domains. However, how bromodomains recognize site-specific histones remains unanswered. Here, we report three three-dimensional solution structures of the bromodomains of the human transcriptional coactivators CREB-binding protein (CBP) and p300/CBP-associated factor (PCAF) bound to peptides derived from histone acetylation sites at lysines 36 and 9 in H3, and lysine 20 in H4. From structural and biochemical binding analyses, we determine consensus histone recognition by the bromodomains of PCAF and CBP, which represent two different subgroups of the bromodomain family. Through bromodomain residues in the ZA and BC loops, PCAF prefers acetylation sites with a hydrophobic residue at (Kac+2) position and a positively charged or aromatic residue at (Kac+3), whereas CBP favors bulky hydrophobic residues at (Kac+1) and (Kac+2), a positively charged residue at (Kac-1), and an aromatic residue at (Kac-2).
The line below this paragraph, {{ABSTRACT_PUBMED_18400184}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18400184 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18400184}}


==About this Structure==
==About this Structure==
2RNX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNX OCA].  
2RNX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RNX OCA].  


==Reference==
==Reference==
Line 48: Line 52:
[[Category: Transcription regulation]]
[[Category: Transcription regulation]]
[[Category: Transferase/nuclear protein complex]]
[[Category: Transferase/nuclear protein complex]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May  7 08:43:33 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:13:47 2008''
Retrieved from "https://proteopedia.org/2rnx"