PDBsum entry 1e5w

Membrane protein

PDB id

1e5w

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Contents

			Protein chain

					346 a.a. *

			Waters ×36

* Residue conservation analysis

PDB id:

1e5w

Links

Name:

Membrane protein

Title:

Structure of isolated ferm domain and first long helix of moesin

Structure:

Moesin. Chain: a. Fragment: ferm domain and helix residue 1-345. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: blr. Other_details: recombinant expression in e.Coli of non-fusion protein

Resolution:

2.70Å

R-factor:

0.254

R-free:

0.297

Authors:

S.D.Edwards,N.H.Keep

Key ref:

S.D.Edwards and N.H.Keep (2001). The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation. Biochemistry, 40, 7061-7068. PubMed id: 11401550

Date:

03-Aug-00

Release date:

27-Jun-01

PROCHECK

	Headers

	References

Protein chain

P26038 (MOES_HUMAN) - Moesin from Homo sapiens

Seq: Struc:

Seq: Struc:					577 a.a. 346 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Biochemistry 40:7061-7068 (2001)
PubMed id: 11401550

The 2.7 A crystal structure of the activated FERM domain of moesin: an analysis of structural changes on activation.
S.D.Edwards, N.H.Keep.

ABSTRACT

Moesin binds to a large range of proteins through its N terminal FERM (band 4.1, ezrin, radixin, moesin) domain. In full-length moesin isolated from cells, this binding is masked by binding to the C-terminal domain of moesin (C-ERMAD). Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which releases the C-ERMAD. A recently determined crystal structure of a noncovalent complex of the FERM and C-ERMAD domains showed for the first time that the structure of the FERM domain consists of three subdomains, each of which is similar to known structures. The structure reported here also contains a unique 47-residue helix pointing away from the FERM domain at the start of the alpha domain, in agreement with secondary structure predictions. Removal of the C-ERMAD does not result in a huge rearrangement of the FERM domain, but comparison with the activated radixin structure shows a consistent set of small changes. Not surprisingly, the exposed C-ERMAD binding area interacts in crystal contacts. More interestingly, a negatively charged peptide binds to the inositol site in a crystal contact and causes a greater conformational change in the structure than inositol.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20001213

C.A.Lipinski, and J.C.Loftus (2010).
Targeting Pyk2 for therapeutic intervention.

Expert Opin Ther Targets, 14, 95.

20546116

K.H.Zawawi, A.Kantarci, U.Schulze-Späte, T.Fujita, E.L.Batista, S.Amar, and T.E.Van Dyke (2010).
Moesin-induced signaling in response to lipopolysaccharide in macrophages.

J Periodontal Res, 45, 589-601.

20308985

R.G.Fehon, A.I.McClatchey, and A.Bretscher (2010).
Organizing the cell cortex: the role of ERM proteins.

Nat Rev Mol Cell Biol, 11, 276-287.

19129194

D.J.Killock, M.Parsons, M.Zarrouk, S.M.Ameer-Beg, A.J.Ridley, D.O.Haskard, M.Zvelebil, and A.Ivetic (2009).
In Vitro and in Vivo Characterization of Molecular Interactions between Calmodulin, Ezrin/Radixin/Moesin, and L-selectin.

J Biol Chem, 284, 8833-8845.

17373875

E.Im, and A.Kazlauskas (2007).
PtdIns-4,5-P2 as a potential therapeutic target for pathologic angiogenesis.

Expert Opin Ther Targets, 11, 443-451.

17218263

K.L.Wegener, A.W.Partridge, J.Han, A.R.Pickford, R.C.Liddington, M.H.Ginsberg, and I.D.Campbell (2007).
Structural basis of integrin activation by talin.

Cell, 128, 171-182.

PDB codes:

2h7d 2h7e

17134719

Q.Li, M.R.Nance, R.Kulikauskas, K.Nyberg, R.Fehon, P.A.Karplus, A.Bretscher, and J.J.Tesmer (2007).
Self-masking in an intact ERM-merlin protein: an active role for the central alpha-helical domain.

J Mol Biol, 365, 1446-1459.

PDB codes:

2i1j 2i1k

16221668

D.F.Ceccarelli, H.K.Song, F.Poy, M.D.Schaller, and M.J.Eck (2006).
Crystal structure of the FERM domain of focal adhesion kinase.

J Biol Chem, 281, 252-259.

PDB codes:

2aeh 2al6

16582480

K.Kitano, F.Yusa, and T.Hakoshima (2006).
Structure of dimerized radixin FERM domain suggests a novel masking motif in C-terminal residues 295-304.

Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 340-345.

PDB code:

2d2q

16324214

K.Golovnina, A.Blinov, E.M.Akhmametyeva, L.V.Omelyanchuk, and L.S.Chang (2005).
Evolution and origin of merlin, the product of the Neurofibromatosis type 2 (NF2) tumor-suppressor gene.

BMC Evol Biol, 5, 69.

16151629

S.Fais, A.De Milito, and F.Lozupone (2005).
The role of FAS to ezrin association in FAS-mediated apoptosis.

Apoptosis, 10, 941-947.

15869386

W.Cho, and R.V.Stahelin (2005).
Membrane-protein interactions in cell signaling and membrane trafficking.

Annu Rev Biophys Biomol Struct, 34, 119-151.

14676203

F.Lozupone, L.Lugini, P.Matarrese, F.Luciani, C.Federici, E.Iessi, P.Margutti, G.Stassi, W.Malorni, and S.Fais (2004).
Identification and relevance of the CD95-binding domain in the N-terminal region of ezrin.

J Biol Chem, 279, 9199-9207.

15169899

J.M.Dunty, V.Gabarra-Niecko, M.L.King, D.F.Ceccarelli, M.J.Eck, and M.D.Schaller (2004).
FERM domain interaction promotes FAK signaling.

Mol Cell Biol, 24, 5353-5368.

15152196

V.Ramesh (2004).
Merlin and the ERM proteins in Schwann cells, neurons and growth cones.

Nat Rev Neurosci, 5, 462-470.

12471164

H.L.Yin, and P.A.Janmey (2003).
Phosphoinositide regulation of the actin cytoskeleton.

Annu Rev Physiol, 65, 761-789.

14529273

K.P.Hoeflich, S.Tsukita, L.Hicks, C.M.Kay, S.Tsukita, and M.Ikura (2003).
Insights into a single rod-like helix in activated radixin required for membrane-cytoskeletal cross-linking.

Biochemistry, 42, 11634-11641.

12517699

S.J.Winder (2003).
Structural insights into actin-binding, branching and bundling proteins.

Curr Opin Cell Biol, 15, 14-22.

12429733

W.J.Smith, N.Nassar, A.Bretscher, R.A.Cerione, and P.A.Karplus (2003).
Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.

J Biol Chem, 278, 4949-4956.

PDB code:

1ni2

12154370

A.Bretscher, K.Edwards, and R.G.Fehon (2002).
ERM proteins and merlin: integrators at the cell cortex.

Nat Rev Mol Cell Biol, 3, 586-599.

11792551

A.Gautreau, D.Louvard, and M.Arpin (2002).
ERM proteins and NF2 tumor suppressor: the Yin and Yang of cortical actin organization and cell growth signaling.

Curr Opin Cell Biol, 14, 104-109.

11856822

B.S.Kang, D.R.Cooper, Y.Devedjiev, U.Derewenda, and Z.S.Derewenda (2002).
The structure of the FERM domain of merlin, the neurofibromatosis type 2 gene product.

Acta Crystallogr D Biol Crystallogr, 58, 381-391.

PDB code:

1h4r

11932255

D.A.Calderwood, B.Yan, J.M.de Pereda, B.G.Alvarez, Y.Fujioka, R.C.Liddington, and M.H.Ginsberg (2002).
The phosphotyrosine binding-like domain of talin activates integrins.

J Biol Chem, 277, 21749-21758.

11784723

J.M.Serrador, M.Vicente-Manzanares, J.Calvo, O.Barreiro, M.C.Montoya, R.Schwartz-Albiez, H.Furthmayr, F.Lozano, and F.Sánchez-Madrid (2002).
A novel serine-rich motif in the intercellular adhesion molecule 3 is critical for its ezrin/radixin/moesin-directed subcellular targeting.

J Biol Chem, 277, 10400-10409.

12142282

M.A.Pufall, and B.J.Graves (2002).
Autoinhibitory domains: modular effectors of cellular regulation.

Annu Rev Cell Dev Biol, 18, 421-462.

11959505

S.Pokutta, and W.I.Weis (2002).
The cytoplasmic face of cell contact sites.

Curr Opin Struct Biol, 12, 255-262.

11756419

T.Shimizu, A.Seto, N.Maita, K.Hamada, S.Tsukita, S.Tsukita, and T.Hakoshima (2002).
Structural basis for neurofibromatosis type 2. Crystal structure of the merlin FERM domain.

J Biol Chem, 277, 10332-10336.

PDB code:

1isn

12136155

W.J.Smith, and R.A.Cerione (2002).
Crystallization and preliminary crystallographic analysis of the ezrin FERM domain.

Acta Crystallogr D Biol Crystallogr, 58, 1359-1361.

11590013

V.Niggli (2001).
Structural properties of lipid-binding sites in cytoskeletal proteins.

Trends Biochem Sci, 26, 604-611.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.