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1p22

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1p22, resolution 2.95Å ()

Non-Standard Residues:

Gene:

CTNNB1 OR CTNNB (Homo sapiens)

Structural annotation:
Resources:	CATH : 1P22A02, 1P22A01, 1P22B00 InterPro : Ipr001810, Ipr011046, Ipr001680, Ipr011333, Ipr001232, Ipr000225, Ipr013284, Ipr011989, Ipr000357 Pfam : PF00646, PF00400, PF03931, PF01466 SCOP : d1p22a1, d1p22a2, d1p22b2, d1p22b1 UniProt : Q9Y297, P63208, P35222

Functional annotation:
Cellular component:	cytoplasm endoplasmic reticulum transcription factor complex plasma membrane basolateral plasma membrane membrane cell-cell adherens junction Z disc beta-catenin destruction complex lamellipodium microvillus membrane membrane fraction lateral plasma membrane apical part of cell cytoskeleton adherens junction nucleus fascia adherens intercellular junction
Biological process:	ubiquitin-dependent protein catabolic process Wnt receptor signaling pathway ubiquitin cycle signal transduction cell adhesion endoderm formation proximal/distal pattern formation synaptic transmission odontogenesis of dentine-containing teeth pancreas development morphogenesis of embryonic epithelium heart development regulation of cell differentiation dorsal/ventral axis specification endodermal cell fate commitment cell fate determination synapse organization and biogenesis negative regulation of transcription from RNA polymerase II promoter cell fate specification camera-type eye morphogenesis embryonic digit morphogenesis osteoclast differentiation cell differentiation hemopoiesis epithelial to mesenchymal transition ectoderm development skeletal development cell maturation positive regulation of osteoblast differentiation cellular morphogenesis during differentiation negative regulation of cell differentiation regulation of cell proliferation positive regulation of epithelial cell differentiation patterning of blood vessels regulation of osteoblast differentiation embryonic arm morphogenesis forebrain development cellular process cell-cell adhesion positive regulation of transcription bone resorption synaptic vesicle transport negative regulation of osteoclast differentiation regulation of transcription, DNA-dependent positive regulation of transcription from RNA polymerase II promoter embryonic hindlimb morphogenesis positive regulation of transcription, DNA-dependent dorsal/ventral pattern formation negative regulation of transcription, DNA-dependent regulation of transcription lung development androgen receptor signaling pathway transcription Wnt receptor signaling pathway through beta-catenin
Molecular function:	protein binding ligase activity protein C-terminus binding chromatin binding cadherin binding DNA binding transcription coactivator activity androgen receptor binding signal transducer activity transcription factor activity binding alpha-catenin binding structural molecule activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

1 Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity on the SCFbeta-TrCP1 ubiquitin ligase
2 About this Structure
3 See Also
4 Reference

Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity on the SCFbeta-TrCP1 ubiquitin ligase

Publication Abstract from PubMed

The SCF ubiquitin ligases catalyze protein ubiquitination in diverse cellular processes. SCFs bind substrates through the interchangeable F box protein subunit, with the >70 human F box proteins allowing the recognition of a wide range of substrates. The F box protein beta-TrCP1 recognizes the doubly phosphorylated DpSGphiXpS destruction motif, present in beta-catenin and IkappaB, and directs the SCF(beta-TrCP1) to ubiquitinate these proteins at specific lysines. The 3.0 A structure of a beta-TrCP1-Skp1-beta-catenin complex reveals the basis of substrate recognition by the beta-TrCP1 WD40 domain. The structure, together with the previous SCF(Skp2) structure, leads to the model of SCF catalyzing ubiquitination by increasing the effective concentration of the substrate lysine at the E2 active site. The model's prediction that the lysine-destruction motif spacing is a determinant of ubiquitination efficiency is confirmed by measuring ubiquitination rates of mutant beta-catenin peptides, solidifying the model and also providing a mechanistic basis for lysine selection.

Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase., Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP, Mol Cell. 2003 Jun;11(6):1445-56. PMID:12820959

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1p22 is a 3 chain structure of Catenin with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Wu G, Xu G, Schulman BA, Jeffrey PD, Harper JW, Pavletich NP. Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol Cell. 2003 Jun;11(6):1445-56. PMID:12820959

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1p22

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Contents

Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity on the SCFbeta-TrCP1 ubiquitin ligase

About this Structure

See Also

Reference

Proteopedia Page Contributors and Editors (what is this?)

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