1mi1

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|GENE=
|GENE=
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02138 Beach], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01201 Neurobeachin]</span>
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam02138 Beach], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd01201 Neurobeachin]</span>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [http://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB]</span>
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mi1 OCA], [http://www.ebi.ac.uk/pdbsum/1mi1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mi1 RCSB]</span>
}}
}}
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[[Category: vesicle trafficking]]
[[Category: vesicle trafficking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 05:56:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:16:18 2008''

Revision as of 19:16, 30 March 2008

Image:1mi1.gif


PDB ID 1mi1

Drag the structure with the mouse to rotate
, resolution 2.90Å
Ligands:
Domains: Beach, Neurobeachin
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the PH-BEACH Domain of Human Neurobeachin


Overview

The BEACH domain is highly conserved in a large family of eukaryotic proteins, and is crucial for their functions in vesicle trafficking, membrane dynamics and receptor signaling. However, it does not share any sequence homology with other proteins. Here we report the crystal structure at 2.9 A resolution of the BEACH domain of human neurobeachin. It shows that the BEACH domain has a new and unusual polypeptide backbone fold, as the peptide segments in its core do not assume regular secondary structures. Unexpectedly, the structure also reveals that the BEACH domain is in extensive association with a novel, weakly conserved pleckstrin-homology (PH) domain. Consistent with the structural analysis, biochemical studies show that the PH and BEACH domains have strong interactions, suggesting they may function as a single unit. Functional studies in intact cells demonstrate the requirement of both the PH and the BEACH domains for activity. A prominent groove at the interface between the two domains may be used to recruit their binding partners.

About this Structure

1MI1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the BEACH domain reveals an unusual fold and extensive association with a novel PH domain., Jogl G, Shen Y, Gebauer D, Li J, Wiegmann K, Kashkar H, Kronke M, Tong L, EMBO J. 2002 Sep 16;21(18):4785-95. PMID:12234919

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