2efl: Difference between revisions

Revision as of 23:22, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2efl.png

Template:STRUCTURE 2efl

Crystal structure of the EFC domain of formin-binding protein 17Crystal structure of the EFC domain of formin-binding protein 17

Template:ABSTRACT PUBMED 17512409

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Mon Jul 28 23:21:58 2008

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OCA

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-'''Crystal structure of the EFC domain of formin-binding protein 17'''
+===Crystal structure of the EFC domain of formin-binding protein 17===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17512409}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17512409 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17512409}}
 ==About this Structure==
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 [[Category: Rsgi]]
 [[Category: Structural genomic]]
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