1mi1
From Proteopedia
(New page: 200px<br /> <applet load="1mi1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mi1, resolution 2.90Å" /> '''Crystal Structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mi1.gif|left|200px]]<br /> | + | [[Image:1mi1.gif|left|200px]]<br /><applet load="1mi1" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1mi1" size=" | + | |
caption="1mi1, resolution 2.90Å" /> | caption="1mi1, resolution 2.90Å" /> | ||
'''Crystal Structure of the PH-BEACH Domain of Human Neurobeachin'''<br /> | '''Crystal Structure of the PH-BEACH Domain of Human Neurobeachin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The BEACH domain is highly conserved in a large family of eukaryotic | + | 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== | ==About this Structure== | ||
| - | 1MI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1MI1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI1 OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 18: | ||
[[Category: Kroenke, M.]] | [[Category: Kroenke, M.]] | ||
[[Category: Li, J.]] | [[Category: Li, J.]] | ||
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Shen, Y.]] | [[Category: Shen, Y.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
| Line 33: | Line 32: | ||
[[Category: vesicle trafficking]] | [[Category: vesicle trafficking]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:21 2008'' |
Revision as of 11:55, 21 February 2008
|
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
Page seeded by OCA on Thu Feb 21 13:55:21 2008
Categories: Homo sapiens | Single protein | Gebauer, D. | Jogl, G. | Kashkar, H. | Kroenke, M. | Li, J. | NESG, Northeast Structural Genomics Consortium. | Shen, Y. | Tong, L. | Wiegmann, K. | Beach domain | Nesg | Northeast structural genomics consortium | Ph domain | Protein structure initiative | Psi | Signal transduction | Structural genomics | Vesicle trafficking
