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Titolo:
Identification and structure of the nerve growth factor binding site on TrkA
Autore:
Robertson, AGS; Banfield, MJ; Allen, SJ; Dando, JA; Mason, GGF; Tyler, SJ; Bennett, GS; Brain, SD; Clarke, AR; Naylor, RL; Wilcock, GK; Brady, RL; Dawbarn, D;
Indirizzi:
Bristol Royal Infirm, URCN, Mol Neurobiol Unit Care Elderly, Bristol BS2 8HW, Avon, England Bristol Royal Infirm Bristol Avon England BS2 8HW BS2 8HW, Avon, England Univ London Kings Coll, Div Biomed Sci, Pharmacol Grp, London SW3 6LX, England Univ London Kings Coll London England SW3 6LX p, London SW3 6LX, England Univ London Kings Coll, Div Biomed Sci, Vasc Biol Res Ctr, London SW3 6LX,England Univ London Kings Coll London England SW3 6LX tr, London SW3 6LX,England Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD Bristol BS8 1TD, Avon, England Frenchay Hosp, Dept Care Elderly, Bristol BS16 1LE, Avon, England FrenchayHosp Bristol Avon England BS16 1LE istol BS16 1LE, Avon, England
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 1, volume: 282, anno: 2001,
pagine: 131 - 141
SICI:
0006-291X(20010323)282:1<131:IASOTN>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
SEPTAL CHOLINERGIC NEURONS; IMMUNOGLOBULIN-LIKE DOMAINS; LEUCINE-RICH MOTIF; ALZHEIMERS-DISEASE; EXTRACELLULAR DOMAIN; NEUROTROPHIN-BINDING; CRYSTAL-STRUCTURES; BASAL FOREBRAIN; RAT SKIN; RECEPTOR;
Keywords:
NGF/TrkA; binding domain; X-ray structure; Alzheimer's disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Robertson, AGS Bristol Royal Infirm, URCN, Mol Neurobiol Unit Care Elderly, Bristol BS2 8HW, Avon, England Bristol Royal Infirm Bristol Avon EnglandBS2 8HW England
Citazione:
A.G.S. Robertson et al., "Identification and structure of the nerve growth factor binding site on TrkA", BIOC BIOP R, 282(1), 2001, pp. 131-141

Abstract

Nerve growth factor (NGF) is involved in the development and maintenance of the nervous system and has been implicated as a possible therapeutic target molecule in a number of neurodegenerative diseases, especially Alzheimer's disease. NGF binds with high affinity to the extracellular region of a tyrosine kinase receptor, TrkA, which comprises three leucine-rich motifs (LRMs), flanked by two cysteine-rich clusters, followed by two immunoglobulin-like (Ig-like) domains. We have expressed the second Ig-like domain as a recombinant protein in E. coil and demonstrate that NGF binds to this domainwith similar affinity to the native receptor. This domain (TrkAIg(2)) has the ability to sequester NGF in vitro, preventing NGF-induced neurite outgrowth, and in vivo, inhibiting NGF-induced plasma extravasation. We also present the three-dimensional structure of the TrkAIg(2) domain in a new crystal form, refined to 2.0 Angstrom resolution. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 13:07:48