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Titolo:
A novel, specific interaction involving the Csk SH3 domain and its naturalligand
Autore:
Ghose, R; Shekhtman, A; Goger, MJ; Ji, H; Cowburn, D;
Indirizzi:
Rockefeller Univ, New York, NY 10021 USA Rockefeller Univ New York NY USA10021 eller Univ, New York, NY 10021 USA New York Struct Biol Ctr, New York, NY 10021 USA New York Struct Biol CtrNew York NY USA 10021 tr, New York, NY 10021 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 11, volume: 8, anno: 2001,
pagine: 998 - 1004
SICI:
1072-8368(200111)8:11<998:ANSIIT>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
TYROSINE PROTEIN-KINASE; MODEL-FREE APPROACH; SINGLE AMINO-ACID; SRC FAMILY; PHOSPHATASE PEP; HIV-1 NEF; CRYSTAL-STRUCTURE; CELL-LINE; C-SRC; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Cowburn, D Rockefeller Univ, 1230 York Ave, New York, NY 10021 USA Rockefeller Univ 1230 York Ave New York NY USA 10021 10021 USA
Citazione:
R. Ghose et al., "A novel, specific interaction involving the Csk SH3 domain and its naturalligand", NAT ST BIOL, 8(11), 2001, pp. 998-1004

Abstract

C-terminal Src kinase (Csk) takes part in a highly specific, high affinityinteraction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells. The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptiderecognition motif involving an SH3 domain. Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobicresidues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP. These two residues are C-terminal to the conventional proline-rich SH3 domain recognition sequence of PEP. This interaction is required in addition to the classic polyproline helix (PPII) recognition by the Csk-SH3 domain for the association between Csk and PEP in vivo. NMR relaxation analysis suggests that Csk-SH3 has different dynamic properties in the various subsites important for peptide recognition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 00:46:14