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Titolo:
The 2.7 angstrom crystal structure of the activated FERM domain of moesin:An analysis of structural changes on activation
Autore:
Edwards, SD; Keep, NH;
Indirizzi:
Univ London Birkbeck Coll, BBSRC Bloomsbury Ctr Struct Biol, London WC1E 7HX, England Univ London Birkbeck Coll London England WC1E 7HX ndon WC1E 7HX, England Univ London Birkbeck Coll, Sch Crystallog, London WC1E 7HX, England Univ London Birkbeck Coll London England WC1E 7HX ndon WC1E 7HX, England
Titolo Testata:
BIOCHEMISTRY
fascicolo: 24, volume: 40, anno: 2001,
pagine: 7061 - 7068
SICI:
0006-2960(20010619)40:24<7061:T2ACSO>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
EZRIN/RADIXIN/MOESIN ERM PROTEINS; AMINO-TERMINAL DOMAIN; ACTIN-BINDING DOMAIN; F-ACTIN; PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE; TUMOR-SUPPRESSOR; EZRIN FAMILY; NF2 GENE; MEMBRANE; ASSOCIATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Keep, NH Univ London Birkbeck Coll, BBSRC Bloomsbury Ctr Struct Biol, Malet St, London WC1E 7HX, England Univ London Birkbeck Coll Malet St London England WC1E 7HX gland
Citazione:
S.D. Edwards e N.H. Keep, "The 2.7 angstrom crystal structure of the activated FERM domain of moesin:An analysis of structural changes on activation", BIOCHEM, 40(24), 2001, pp. 7061-7068

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-ERNIAD). Activation takes place by phosphorylation of Thr 558 in the C-ERMAD, which releases the C-IERMAD. A recently determined crystal structureof 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 herealso contains a unique 47-residue helix pointing away from the FERM domainat the start of the a 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 23:11:00