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Messaggio inserito da Fiammella85

Vorrei porre alcune domande a chi mi sa rispondere:
1-cos'č il dominio WD contenuto nella proteina MEP50

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WDR1 WD repeat domain 1

WD repeats are approximately 30- to 40-amino acid domains containing several conserved residues, mostly including a trp-asp at the C-terminal end. WD domains are involved in protein-protein interactions.

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Coronin

These domains were discovered in 1986 and are characterized by a partial conserved domain of 40-60 amino acids, starting with GH dipeptide 11-24 residue away from the N-terminus and ending with a tryptophane-aspartic acid (WD) dipeptide at the C-terminus. The WD domain has no intrinsic catalytic activity and is thought to serve as a stable platform for simultaneous interaction. WD repeat proteins have diverse cellular functions. They play central role in physiological processes like signal transduction, transcriptional regulation, cytoskeleton remodeling, regulation of vesicle trafficking etc.

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The WD40 Domain has been observed as a structural motif of 40-43 amino acids in the beta subunit of G-proteins (Fong et al, 1986). It helps to form a circular propeller-like structure with a central pore (Lambright et al, 1996; Sondek et al, 1996; Garcia-Higuera et al, 1996). The seven blades of the propeller and the platform formed by them are potential binding surfaces for proteins and/or small ligands, which can bind either stably or reversibly (Smith et al, 1999).

WD40 repeats have been found in a number of eukaryotic proteins, including adaptor/regulatory modules in signal transduction, pre-mRNA processing, cytoskeleton assembly and cell cycle control (Paroush et al, 1994; Komachi and Johnson, 1997; Tyers and Jorgensen, 2000).

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