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.


1ul1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ul1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ul1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ul1| PDB=1ul1 | SCENE= }}
{{STRUCTURE_1ul1| PDB=1ul1 | SCENE= }}
-
'''Crystal structure of the human FEN1-PCNA complex'''
+
===Crystal structure of the human FEN1-PCNA complex===
-
==Overview==
+
<!--
-
Flap endonuclease-1 (FEN1) is a key enzyme for maintaining genomic stability and replication. Proliferating cell nuclear antigen (PCNA) binds FEN1 and stimulates its endonuclease activity. The structural basis of the FEN1-PCNA interaction was revealed by the crystal structure of the complex between human FEN1 and PCNA. The main interface involves the C-terminal tail of FEN1, which forms two beta-strands connected by a short helix, the betaA-alphaA-betaB motif, participating in beta-beta and hydrophobic interactions with PCNA. These interactions are similar to those previously observed for the p21CIP1/WAF1 peptide. However, this structure involving the full-length enzyme has revealed additional interfaces that are involved in the core domain. The interactions at the interfaces maintain the enzyme in an inactive 'locked-down' orientation and might be utilized in rapid DNA-tracking by preserving the central hole of PCNA for sliding along the DNA. A hinge region present between the core domain and the C-terminal tail of FEN1 would play a role in switching the FEN1 orientation from an inactive to an active orientation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15616578}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15616578 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15616578}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Replication]]
[[Category: Replication]]
[[Category: Sliding clamp]]
[[Category: Sliding clamp]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:22:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:12:57 2008''

Revision as of 23:13, 28 July 2008

Template:STRUCTURE 1ul1

Crystal structure of the human FEN1-PCNA complex

Template:ABSTRACT PUBMED 15616578

About this Structure

1UL1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for recruitment of human flap endonuclease 1 to PCNA., Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, Fukuda K, Uchida M, Ohtsuka E, Morioka H, Hakoshima T, EMBO J. 2005 Feb 23;24(4):683-93. Epub 2004 Dec 16. PMID:15616578

Page seeded by OCA on Tue Jul 29 02:12:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools