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1jpp

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1jpp, resolution 3.10Å ()

Sites:

Ligands:

Structural annotation:
Resources:	CATH : 1Jppa00, 1Jppb00 InterPro : Ipr000225, Ipr013284, Ipr011989, Ipr000357, Ipr009223, Ipr009224, Ipr009232, Ipr009240, Ipr009234 Pfam : PF02985, PF00514, PF05972 SCOP : d1jppa_, d1jppb_ UniProt : Q02248, P25054

Functional annotation:
Cellular component:	cytoskeleton apical part of cell lateral plasma membrane transcription factor complex membrane cell-cell adherens junction adherens junction Z disc membrane fraction cytoplasm basolateral plasma membrane microvillus membrane nucleus fascia adherens lamellipodium plasma membrane apical junction complex beta-catenin destruction complex intercellular junction centrosome kinetochore
Biological process:	positive regulation of epithelial cell differentiation skeletal development hemopoiesis synaptic vesicle transport dorsal/ventral axis specification cell fate specification synapse organization and biogenesis endodermal cell fate commitment regulation of osteoblast differentiation Wnt receptor signaling pathway negative regulation of osteoclast differentiation lung development ectoderm development negative regulation of chondrocyte differentiation morphogenesis of embryonic epithelium synaptic transmission odontogenesis of dentine-containing teeth transcription cell differentiation cell-cell adhesion cell adhesion patterning of blood vessels negative regulation of transcription, DNA-dependent dorsal/ventral pattern formation cellular morphogenesis during differentiation negative regulation of cell differentiation regulation of transcription regulation of cell proliferation positive regulation of transcription from RNA polymerase II promoter regulation of transcription, DNA-dependent bone resorption proximal/distal pattern formation camera-type eye morphogenesis cell maturation positive regulation of transcription, DNA-dependent positive regulation of osteoblast differentiation embryonic arm morphogenesis osteoclast differentiation endoderm formation embryonic hindlimb morphogenesis forebrain development heart development pancreas development cellular process negative regulation of transcription from RNA polymerase II promoter positive regulation of transcription cell fate determination Wnt receptor signaling pathway through beta-catenin embryonic digit morphogenesis regulation of cell differentiation protein complex assembly regulation of attachment of spindle microtubules to kinetochore negative regulation of cell cycle anterior/posterior pattern formation negative regulation of cell proliferation axis specification cell cycle arrest negative regulation of microtubule depolymerization negative regulation of cyclin-dependent protein kinase activity cell cycle response to DNA damage stimulus
Molecular function:	binding protein binding chromatin binding protein C-terminus binding double-stranded DNA binding cadherin binding alpha-catenin binding structural molecule activity transcription activator activity transcription coactivator activity DNA binding transcription factor binding transcription factor activity beta-catenin binding microtubule binding protein kinase binding protein kinase CK2 regulator 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 The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin
2 About this Structure
3 See Also
4 Reference

The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin

Publication Abstract from PubMed

The adenomatous polyposis coli (APC) tumor suppressor protein plays a critical role in regulating cellular levels of the oncogene product beta-catenin. APC binds to beta-catenin through a series of homologous 15 and 20 amino acid repeats. We have determined the crystal structure of a 15 amino acid beta-catenin binding repeat from APC bound to the armadillo repeat region of beta-catenin. Although it lacks significant sequence homology, the N-terminal half of the repeat binds in a manner similar to portions of E-cadherin and XTcf3, but the remaining interactions are unique to APC. We discuss the implications of this new structure for the design of therapeutics, and present evidence from structural, biochemical and sequence data, which suggest that the 20 amino acid repeats can adopt two modes of binding to beta-catenin.

Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex., Eklof Spink K, Fridman SG, Weis WI, EMBO J. 2001 Nov 15;20(22):6203-12. PMID:11707392

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

About this Structure

1jpp is a 4 chain structure of Catenin with sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Eklof Spink K, Fridman SG, Weis WI. Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex. EMBO J. 2001 Nov 15;20(22):6203-12. PMID:11707392 doi:10.1093/emboj/20.22.6203

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1jpp

From Proteopedia

Contents

The Structure of a beta-Catenin Binding Repeat from Adenomatous Polyposis Coli (APC) in Complex with beta-Catenin

About this Structure

See Also

Reference

Proteopedia Page Contributors and Editors (what is this?)

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