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Titolo:
Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2
Autore:
Hamada, K; Shimizu, T; Matsui, T; Tsukita, S; Tsukita, S; Hakoshima, T;
Indirizzi:
Nara Inst Sci & Technol, Dept Mol Biol, Nara 6300101, Japan Nara Inst Sci & Technol Nara Japan 6300101 Mol Biol, Nara 6300101, Japan Kyoto Univ, Fac Med, Dept Cell Biol, Sakyo Ku, Kyoto 6068315, Japan Kyoto Univ Kyoto Japan 6068315 Cell Biol, Sakyo Ku, Kyoto 6068315, Japan KAN Res Inst, Shimogyo Ku, Kyoto 6008317, Japan KAN Res Inst Kyoto Japan6008317 Inst, Shimogyo Ku, Kyoto 6008317, Japan Kyoto Univ, Coll Med Technol, Sakyo Ku, Kyoto 6068507, Japan Kyoto Univ Kyoto Japan 6068507 d Technol, Sakyo Ku, Kyoto 6068507, Japan
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 57, anno: 2001,
parte:, 6
pagine: 891 - 892
SICI:
0907-4449(200106)57:<891:CCOTRF>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
EZRIN/RADIXIN/MOESIN ERM PROTEINS; ACTIN-BASED CYTOSKELETONS; CLEAVAGE FURROW; MOESIN; EZRIN; FAMILY; LOCALIZATION; ASSOCIATION; CELLS; CD44;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
19
Recensione:
Indirizzi per estratti:
Indirizzo: Hakoshima, T Nara Inst Sci & Technol, Dept Mol Biol, 8916-5 Takayama, Nara6300101, Japan Nara Inst Sci & Technol 8916-5 Takayama Nara Japan 6300101n
Citazione:
K. Hamada et al., "Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2", ACT CRYST D, 57, 2001, pp. 891-892

Abstract

Radixin is a member of the ERM proteins, which cross-link plasma membranesand actin filaments. The FERM domains located at the N-terminal regions ofERM proteins are responsible for membrane association through direct interactions with the cytoplasmic domains of integral membrane proteins. Here, crystals of the complex between the radixin FERM domain and the full-length cytoplasmic tail (28-residue peptide) of intercellular adhesion molecule 2,ICAM-2, have been obtained. The crystals were found to belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 100.44 (9), c = 99.49 (6) Angstrom, and contain one complex in the crystallographic asymmetric unit. An intensity data set was collected to a resolution of 2.60 Angstrom.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 23:08:27