2efk

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{{STRUCTURE_2efk| PDB=2efk | SCENE= }}
{{STRUCTURE_2efk| PDB=2efk | SCENE= }}
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'''Crystal structure of the EFC domain of Cdc42-interacting protein 4'''
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===Crystal structure of the EFC domain of Cdc42-interacting protein 4===
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==Overview==
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Pombe Cdc15 homology (PCH) proteins play an important role in a variety of actin-based processes, including clathrin-mediated endocytosis (CME). The defining feature of the PCH proteins is an evolutionarily conserved EFC/F-BAR domain for membrane association and tubulation. In the present study, we solved the crystal structures of the EFC domains of human FBP17 and CIP4. The structures revealed a gently curved helical-bundle dimer of approximately 220 A in length, which forms filaments through end-to-end interactions in the crystals. The curved EFC dimer fits a tubular membrane with an approximately 600 A diameter. We subsequently proposed a model in which the curved EFC filament drives tubulation. In fact, striation of tubular membranes was observed by phase-contrast cryo-transmission electron microscopy, and mutations that impaired filament formation also impaired membrane tubulation and cell membrane invagination. Furthermore, FBP17 is recruited to clathrin-coated pits in the late stage of CME, indicating its physiological role.
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{{ABSTRACT_PUBMED_17512409}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:28:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:02:18 2008''

Revision as of 11:02, 28 July 2008

Image:2efk.png

Template:STRUCTURE 2efk

Crystal structure of the EFC domain of Cdc42-interacting protein 4

Template:ABSTRACT PUBMED 17512409

About this Structure

2EFK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis., Shimada A, Niwa H, Tsujita K, Suetsugu S, Nitta K, Hanawa-Suetsugu K, Akasaka R, Nishino Y, Toyama M, Chen L, Liu ZJ, Wang BC, Yamamoto M, Terada T, Miyazawa A, Tanaka A, Sugano S, Shirouzu M, Nagayama K, Takenawa T, Yokoyama S, Cell. 2007 May 18;129(4):761-72. PMID:17512409

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