2q13
From Proteopedia
(New page: 200px<br /> <applet load="2q13" size="450" color="white" frame="true" align="right" spinBox="true" caption="2q13, resolution 2.05Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2q13. | + | [[Image:2q13.jpg|left|200px]]<br /><applet load="2q13" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2q13" size=" | + | |
caption="2q13, resolution 2.05Å" /> | caption="2q13, resolution 2.05Å" /> | ||
'''Crystal structure of BAR-PH domain of APPL1'''<br /> | '''Crystal structure of BAR-PH domain of APPL1'''<br /> | ||
| Line 8: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2Q13 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:// | + | 2Q13 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=2Q13 OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 21: | ||
[[Category: protein transport]] | [[Category: protein transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:12:57 2008'' |
Revision as of 12:12, 23 January 2008
|
Crystal structure of BAR-PH domain of APPL1
Overview
APPL1 is an effector of the small GTPase Rab5. Together, they mediate a, signal transduction pathway initiated by ligand binding to cell surface, receptors. Interaction with Rab5 is confined to the amino (N)-terminal, region of APPL1. We report the crystal structures of human APPL1, N-terminal BAR-PH domain motif. The BAR and PH domains, together with a, novel linker helix, form an integrated, crescent-shaped, symmetrical, dimer. This BAR-PH interaction is likely conserved in the class of BAR-PH, containing proteins. Biochemical analyses indicate two independent, Rab-binding sites located at the opposite ends of the dimer, where the PH, domain directly interacts with Rab5 and Rab21. Besides structurally, supporting the PH domain, the BAR domain also contributes to Rab binding, through a small surface region in the vicinity of the PH domain. In stark, contrast to the helix-dominated, Rab-binding domains previously reported, APPL1 PH domain employs beta-strands to interact with Rab5. On the Rab5, side, both switch regions are involved in the interaction. Thus we, identified a new binding mode between PH domains and small GTPases.
About this Structure
2Q13 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the APPL1 BAR-PH domain and characterization of its interaction with Rab5., Zhu G, Chen J, Liu J, Brunzelle JS, Huang B, Wakeham N, Terzyan S, Li X, Rao Z, Li G, Zhang XC, EMBO J. 2007 Jul 25;26(14):3484-93. Epub 2007 Jun 21. PMID:17581628
Page seeded by OCA on Wed Jan 23 14:12:57 2008
