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Titolo:
CRYSTAL-STRUCTURE OF THE EXTRACELLULAR DOMAIN FROM P-0, THE MAJOR STRUCTURAL PROTEIN OF PERIPHERAL-NERVE MYELIN
Autore:
SHAPIRO L; DOYLE JP; HENSLEY P; COLMAN DR; HENDRICKSON WA;
Indirizzi:
COLUMBIA UNIV,DEPT BIOCHEM & MOL BIOPHYS,630 W 168TH ST NEW YORK NY 10032 COLUMBIA UNIV,HOWARD HUGHES MED INST NEW YORK NY 10032 CUNY MT SINAI SCH MED,BROOKDALE CTR MOL BIOL NEW YORK NY 10029 SMITHKLINE BEECHAM PHARMACEUT,DEPT MACROMOL SCI KING OF PRUSSIA PA 19406
Titolo Testata:
Neuron
fascicolo: 3, volume: 17, anno: 1996,
pagine: 435 - 449
SICI:
0896-6273(1996)17:3<435:COTEDF>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
TOOTH NEUROPATHY TYPE-1; CELL-ADHESION MOLECULE; FREEZE-FRACTURE; MEMBRANE INTERACTIONS; SURFACE-CHARGE; SOLUBLE FORM; HUMAN CD4; PO GENE; RESOLUTION; FRAGMENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
58
Recensione:
Indirizzi per estratti:
Citazione:
L. Shapiro et al., "CRYSTAL-STRUCTURE OF THE EXTRACELLULAR DOMAIN FROM P-0, THE MAJOR STRUCTURAL PROTEIN OF PERIPHERAL-NERVE MYELIN", Neuron, 17(3), 1996, pp. 435-449

Abstract

P-0, the major protein of peripheral nerve myelin, mediates membrane adhesion in the spiral wraps of the myelin sheath. We have determined the crystal structure of the extracellular domain from P-0 (P(0)ex) at1.9 Angstrom resolution. P(0)ex is folded like a typical immunoglobulin variable-like domain; five residues at the C-terminus are disordered, suggesting a flexible linkage to the membrane. The requirements forcrystallization of P(0)ex are similar to those for maintaining the native extracellular spacing of adjacent myelin lamellae; thus, given the self-adhesive character of P(0)ex, the crystal itself may reveal some of the natural interactions that occur between P-0 molecules in myelin. The structure leads to the suggestion that P-0 extracellular domains may emanate from the membrane surface as tetramers that link to tetramers on the opposing membrane surface, to result in the formation ofnetworks of molecules. We report analytical ultracentrifugation data for P(0)ex that support this idea.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 06:02:30