1INZ

SOLUTION STRUCTURE OF THE EPSIN N-TERMINAL HOMOLOGY (ENTH) DOMAIN OF HUMAN EPSIN

Summary for 1INZ

• Entry DOI: 10.2210/pdb1inz/pdb
• NMR Information: BMRB: 4959
• Descriptor: EPS15-INTERACTING PROTEIN(EPSIN) (1 entity in total)
• Functional Keywords: alpha-helix, epsin, riken structural genomics/proteomics initiative, rsgi, structural genomics, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 17308.64

Authors

Koshiba, S.,Kigawa, T.,Kikuchi, A.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2000-12-05, release date: 2001-05-09, Last modification date: 2023-12-27)

Primary citation

Koshiba, S.,Kigawa, T.,Kikuchi, A.,Yokoyama, S.
Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin
J.STRUCT.FUNCT.GENOM., 2:1-8, 2001

PubMed Abstract: Epsin is a protein that binds to the Eps15 homology (EH) domains, and is involved in clathrin-mediated endocytosis. The epsin N-terminal homology (ENTH) domain (about 140 amino acid residues) is well conserved in eukaryotes and is considered to be important for actin cytoskeleton organization in endocytosis. In this study, we have determined the solution structure of the ENTH domain (residues 1-144) of human epsin by multidimensional nuclear magnetic resonance spectroscopy. In the ENTH-domain structure, seven alpha-helices form a superhelical fold, consisting of two antiparallel two-helix HEAT motifs and one three-helix ARM motif, with a continuous hydrophobic core in the center. We conclude that the seven-helix superhelical fold defines the ENTH domain, and that the previously-reported eight-helix fold of a longer fragment of rat epsin 1 is divided into the authentic ENTH domain and a C-terminal flanking alpha-helix.

PubMed: 12836669
DOI: 10.1023/A:1011397007366

Experimental method

SOLUTION NMR