1ldd: Difference between revisions

Revision as of 12:32, 2 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:1ldd.png

Template:STRUCTURE 1ldd

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase ComplexStructure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex

Template:ABSTRACT PUBMED 11961546

About this StructureAbout this Structure

1LDD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex., Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP, Nature. 2002 Apr 18;416(6882):703-9. PMID:11961546

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OCA

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 {{STRUCTURE_1ldd|  PDB=1ldd  |  SCENE=  }}
-'''Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex'''
+===Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF Ubiquitin Ligase Complex===
-==Overview==
+<!--
-SCF complexes are the largest family of E3 ubiquitin-protein ligases and mediate the ubiquitination of diverse regulatory and signalling proteins. Here we present the crystal structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF complex, which shows that Cul1 is an elongated protein that consists of a long stalk and a globular domain. The globular domain binds the RING finger protein Rbx1 through an intermolecular beta-sheet, forming a two-subunit catalytic core that recruits the ubiquitin-conjugating enzyme. The long stalk, which consists of three repeats of a novel five-helix motif, binds the Skp1-F boxSkp2 protein substrate-recognition complex at its tip. Cul1 serves as a rigid scaffold that organizes the Skp1-F boxSkp2 and Rbx1 subunits, holding them over 100 A apart. The structure suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold.
+The line below this paragraph, {{ABSTRACT_PUBMED_11961546}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11961546 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11961546}}
 ==About this Structure==
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 [[Category: Ubiquitination]]
 [[Category: Winged-helix]]
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