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.


1dh3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dh3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dh3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dh3| PDB=1dh3 | SCENE= }}
{{STRUCTURE_1dh3| PDB=1dh3 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING'''
+
===CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING===
-
==Overview==
+
<!--
-
The cAMP responsive element-binding protein (CREB) is central to second messenger regulated transcription. To elucidate the structural mechanisms of DNA binding and selective dimerization of CREB, we determined to 3.0 A resolution, the structure of the CREB bZIP (residues 283-341) bound to a 21-base pair deoxynucleotide that encompasses the canonical 8-base pair somatostatin cAMP response element (SSCRE). The CREB dimer is stabilized in part by ionic interactions from Arg(314) to Glu(319') and Glu(328) to Lys(333') as well as a hydrogen bond network that links the carboxamide side chains of Gln(322')-Asn(321)-Asn(321')-Gln(322). Critical to family selective dimerization are intersubunit hydrogen bonds between basic region residue Tyr(307) and leucine zipper residue Glu(312), which are conserved in all CREB/CREM/ATF-1 family members. Strikingly, the structure reveals a hexahydrated Mg(2+) ion bound in the cavity between the basic region and SSCRE that makes a water-mediated DNA contact. DNA binding studies demonstrate that Mg(2+) ions enhance CREB bZIP:SSCRE binding by more than 25-fold and suggest a possible physiological role for this ion in somatostatin cAMP response element and potentially other CRE-mediated gene expression.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10952992}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10952992 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10952992}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Schumacher, M A.]]
[[Category: Schumacher, M A.]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:04:04 2008''

Revision as of 20:04, 30 June 2008

Template:STRUCTURE 1dh3

CRYSTAL STRUCTURE OF A CREB BZIP-CRE COMPLEX REVEALS THE BASIS FOR CREB FAIMLY SELECTIVE DIMERIZATION AND DNA BINDING

Template:ABSTRACT PUBMED 10952992

About this Structure

1DH3 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding., Schumacher MA, Goodman RH, Brennan RG, J Biol Chem. 2000 Nov 10;275(45):35242-7. PMID:10952992

Page seeded by OCA on Mon Jun 30 23:04:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools