1ni2
From Proteopedia
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| - | [[Image:1ni2.gif|left|200px]] | + | [[Image:1ni2.gif|left|200px]] |
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| - | '''Structure of the active FERM domain of Ezrin''' | + | {{Structure |
| + | |PDB= 1ni2 |SIZE=350|CAPTION= <scene name='initialview01'>1ni2</scene>, resolution 2.30Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= VIL2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Structure of the active FERM domain of Ezrin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NI2 is a [ | + | 1NI2 is a [[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=1NI2 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions., Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA, J Biol Chem. 2003 Feb 14;278(7):4949-56. Epub 2002 Nov 11. PMID:[http:// | + | Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions., Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA, J Biol Chem. 2003 Feb 14;278(7):4949-56. Epub 2002 Nov 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12429733 12429733] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ubiquitin-like domain]] | [[Category: ubiquitin-like domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:57:10 2008'' |
Revision as of 10:57, 20 March 2008
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| , resolution 2.30Å | |||||||
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| Gene: | VIL2 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the active FERM domain of Ezrin
Overview
Ezrin is a member of the ERM (ezrin, radixin, moesin) family of proteins that cross-link the actin cytoskeleton to the plasma membrane and also may function in signaling cascades that regulate the assembly of actin stress fibers. Here, we report a crystal structure for the free (activated) FERM domain (residues 2-297) of recombinant human ezrin at 2.3 A resolution. Structural comparison among the dormant moesin FERM domain structure and the three known active FERM domain structures (radixin, moesin, and now ezrin) allows the clear definition of regions that undergo structural changes during activation. The key regions affected are residues 135-150 and 155-180 in lobe F2 and residues 210-214 and 235-267 in lobe F3. Furthermore, we show that a large increase in the mobilities of lobes F2 and F3 accompanies activation, suggesting that their integrity is compromised. This leads us to propose a new concept that we refer to as keystone interactions. Keystone interactions occur when one protein (or protein part) contributes residues that allow another protein to complete folding, meaning that it becomes an integral part of the structure and would rarely dissociate. Such interactions are well suited for long-lived cytoskeletal protein interactions. The keystone interactions concept leads us to predict two specific docking sites within lobes F2 and F3 that are likely to bind target proteins.
About this Structure
1NI2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions., Smith WJ, Nassar N, Bretscher A, Cerione RA, Karplus PA, J Biol Chem. 2003 Feb 14;278(7):4949-56. Epub 2002 Nov 11. PMID:12429733
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