1EDU

CRYSTAL STRUCTURE OF THE ENTH DOMAIN OF RAT EPSIN 1

Summary for 1EDU

• Entry DOI: 10.2210/pdb1edu/pdb
• Descriptor: EH domain binding protein EPSIN, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: alpha-helix, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: O88339
• Total number of polymer chains: 1
• Total formula weight: 17808.25

Authors

Hyman, J.H.,Chen, H.,Decamilli, P.,Brunger, A.T. (deposition date: 2000-01-28, release date: 2000-05-10, Last modification date: 2024-11-06)

Primary citation

Hyman, J.,Chen, H.,Di Fiore, P.P.,De Camilli, P.,Brunger, A.T.
Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and HEAT repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF).
J.Cell Biol., 149:537-546, 2000

PubMed Abstract: Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1- dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function.

PubMed: 10791968
DOI: 10.1083/jcb.149.3.537

Experimental method

X-RAY DIFFRACTION (1.8 Å)