We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1owr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1owr.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1owr.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1owr| PDB=1owr | SCENE= }}
{{STRUCTURE_1owr| PDB=1owr | SCENE= }}
-
'''CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA'''
+
===CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA===
-
==Overview==
+
<!--
-
The nuclear factor of activated T cells (NFAT) is a calcium-dependent transcription factor that cooperates with a myriad of partner transcription factors to regulate distinct transcription programs. Transcription activation by NFAT without the cooperation of co-stimulatory signals in lymphocytes can also impose a genetic program of anergy. Although the ternary NFAT1/Fos-Jun/DNA complex has been structurally characterized, how NFAT1 recognizes DNA in the absence of cooperative partners and how such a binary NFAT/DNA complex may lead to the assembly of distinct high-order NFAT transcription complexes are still poorly understood. We have determined the crystal structure of the entire Rel homology region (RHR) of human NFAT1 (NFATc2) bound to DNA as a monomer. We also present footprinting evidence that corroborates the protein-DNA contacts observed in the crystal structure. Our structural and biochemical studies reveal the mechanism by which the monomeric Rel protein NFAT recognizes its cognate DNA site. A remarkable feature of the binary NFAT/DNA complex is the conformational flexibility exhibited by NFAT1 in the four independent copies of the NFAT/DNA complex in the crystal structure, which may reflect a mechanism by which NFAT1 interacts with a variety of protein partners as it mediates disparate biological responses.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14643663}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14643663 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14643663}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Pseudo-continuous]]
[[Category: Pseudo-continuous]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:22:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:44:36 2008''

Revision as of 05:44, 28 July 2008

Image:1owr.png

Template:STRUCTURE 1owr

CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA

Template:ABSTRACT PUBMED 14643663

About this Structure

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

Reference

Structure of NFAT bound to DNA as a monomer., Stroud JC, Chen L, J Mol Biol. 2003 Dec 12;334(5):1009-22. PMID:14643663

Page seeded by OCA on Mon Jul 28 08:44:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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