1f9f: Difference between revisions

Revision as of 02:54, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f9f.png

Template:STRUCTURE 1f9f

CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAINCRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN

Template:ABSTRACT PUBMED 10906136

About this StructureAbout this Structure

1F9F is a Single protein structure of sequence from Human papillomavirus type 18. Full crystallographic information is available from OCA.

ReferenceReference

The structural basis of DNA target discrimination by papillomavirus E2 proteins., Kim SS, Tam JK, Wang AF, Hegde RS, J Biol Chem. 2000 Oct 6;275(40):31245-54. PMID:10906136

Page seeded by OCA on Tue Jul 1 02:54:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1f9f.gif|left|200px]]
+{{Seed}}
+[[Image:1f9f.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1f9f|  PDB=1f9f  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN'''
+===CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN===
-==Overview==
+<!--
-The papillomavirus E2 proteins regulate the transcription of all papillomavirus genes and are necessary for viral DNA replication. Disruption of the E2 gene is commonly associated with malignancy in cervical carcinoma, indicating that E2 has a role in regulating tumor progression. Although the E2 proteins from all characterized papillomaviruses bind specifically to the same 12-base pair DNA sequence, the cancer-associated human papillomavirus E2 proteins display a unique ability to detect DNA flexibility and intrinsic curvature. To understand the structural basis for this phenomenon, we have determined the crystal structures of the human papillomavirus-18 E2 DNA-binding domain and its complexes with high and low affinity binding sites. The E2 protein is a dimeric beta-barrel and the E2-DNA interaction is accompanied by a large deformation of the DNA as it conforms to the E2 surface. DNA conformation and E2-DNA contacts are similar in both high and low affinity complexes. The differences in affinity correlate with the flexibility of the DNA sequence. Preferences of E2 proteins from different papillomavirus strains for flexible or prevent DNA targets correlate with the distribution of positive charge on their DNA interaction surfaces, suggesting a role for electrostatic forces in the recognition of DNA deformability.
+The line below this paragraph, {{ABSTRACT_PUBMED_10906136}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10906136 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10906136}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Dna-binding]]
 [[Category: Trans-acting factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:03:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 02:54:38 2008''