1mi1: Difference between revisions

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[[Image:1mi1.~~gif~~|left|200px]]

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~~'''~~Crystal Structure of the PH-BEACH Domain of Human Neurobeachin~~'''~~

===Crystal Structure of the PH-BEACH Domain of Human Neurobeachin===

~~==Overview==~~

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_12234919}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12234919 is the PubMed ID number.

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==About this Structure==

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[[Category: Structural genomic]]

[[Category: Vesicle trafficking]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ 3 01:04:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:00:51 2008''

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-[[Image:1mi1.gif|left|200px]]
+{{Seed}}
+[[Image:1mi1.png|left|200px]]
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 {{STRUCTURE_1mi1|  PDB=1mi1  |  SCENE=  }}
-'''Crystal Structure of the PH-BEACH Domain of Human Neurobeachin'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12234919}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12234919 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12234919}}
 ==About this Structure==
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 [[Category: Structural genomic]]
 [[Category: Vesicle trafficking]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:04:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:00:51 2008''