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.


2azm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2azm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2azm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2azm| PDB=2azm | SCENE= }}
{{STRUCTURE_2azm| PDB=2azm | SCENE= }}
-
'''Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX'''
+
===Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX===
-
==Overview==
+
<!--
-
Histone variant H2AX phosphorylation in response to DNA damage is the major signal for recruitment of DNA-damage-response proteins to regions of damaged chromatin. Loss of H2AX causes radiosensitivity, genome instability, and DNA double-strand-break repair defects, yet the mechanisms underlying these phenotypes remain obscure. Here, we demonstrate that mammalian MDC1/NFBD1 directly binds to phospho-H2AX (gammaH2AX) by specifically interacting with the phosphoepitope at the gammaH2AX carboxyl terminus. Moreover, through a combination of biochemical, cell-biological, and X-ray crystallographic approaches, we reveal the molecular details of the MDC1/NFBD1-gammaH2AX complex. These data provide compelling evidence that the MDC1/NFBD1 BRCT repeat domain is the major mediator of gammaH2AX recognition following DNA damage. We further show that MDC1/NFBD1-gammaH2AX complex formation regulates H2AX phosphorylation and is required for normal radioresistance and efficient accumulation of DNA-damage-response proteins on damaged chromatin. Thus, binding of MDC1/NFBD1 to gammaH2AX plays a central role in the mammalian response to DNA damage.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16377563}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16377563 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16377563}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Dna damage]]
[[Category: Dna damage]]
[[Category: Protein-phosphopeptide complex]]
[[Category: Protein-phosphopeptide complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:39:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:14:36 2008''

Revision as of 10:14, 27 July 2008

Image:2azm.png

Template:STRUCTURE 2azm

Crystal structure of the MDC1 brct repeat in complex with the histone tail of gamma-H2AX

Template:ABSTRACT PUBMED 16377563

About this Structure

2AZM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks., Stucki M, Clapperton JA, Mohammad D, Yaffe MB, Smerdon SJ, Jackson SP, Cell. 2005 Dec 29;123(7):1213-26. PMID:16377563

Page seeded by OCA on Sun Jul 27 13:14:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2azm"
Personal tools