The mouse Major Urinary Proteins (MUPs), known also as Mus m 1 urinary allergen complex , are lipocalins involved in pheromonal signalling. The 3D structure of a recombinant member of this protein family, rMUP, has been determined by NMR spectroscopy and crystallography. The lipocalin fold creates an internal cavity recognized as the binding site for a range of hydrophobic ligands acting as chemosignals perceived by conspecifics. It was previously suggested that the binding of ligands inside the pocket relies upon the formation of a network of interactions with selected protein side chains. The aim of this work is to elucidate the functional and structural role of Tyr120 whose side chain appears to interact with the bound pheromone 2-sec-buthyl-thyazoline. By site-specific mutagenesis this residue was replaced with Phe (rMUP-Y120F) and Ala (rMUPY120A). Fluorescence and CD spectroscopy data taken together with guanidinium chloride denaturation results show that Tyr120 not only plays an important role in the binding process but also is a key residue in the stabilization of the protein architecture.

Structural Analysis of Mutants of the Mouse Major Urinary Protein / Casali, Emanuela; Ferrari, Elena; Venturelli, M. B.; Sartor, G.; Spisni, Alberto. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - 53 (3):(2004), pp. 339-339. (Intervento presentato al convegno 49° Congresso Nazionale della Società Italiana di Biochimica e Biologia Molecolare tenutosi a Riccione, Italy nel 28 September -1 October 2004).

Structural Analysis of Mutants of the Mouse Major Urinary Protein

CASALI, Emanuela;FERRARI, Elena;SPISNI, Alberto
2004-01-01

Abstract

The mouse Major Urinary Proteins (MUPs), known also as Mus m 1 urinary allergen complex , are lipocalins involved in pheromonal signalling. The 3D structure of a recombinant member of this protein family, rMUP, has been determined by NMR spectroscopy and crystallography. The lipocalin fold creates an internal cavity recognized as the binding site for a range of hydrophobic ligands acting as chemosignals perceived by conspecifics. It was previously suggested that the binding of ligands inside the pocket relies upon the formation of a network of interactions with selected protein side chains. The aim of this work is to elucidate the functional and structural role of Tyr120 whose side chain appears to interact with the bound pheromone 2-sec-buthyl-thyazoline. By site-specific mutagenesis this residue was replaced with Phe (rMUP-Y120F) and Ala (rMUPY120A). Fluorescence and CD spectroscopy data taken together with guanidinium chloride denaturation results show that Tyr120 not only plays an important role in the binding process but also is a key residue in the stabilization of the protein architecture.
2004
Structural Analysis of Mutants of the Mouse Major Urinary Protein / Casali, Emanuela; Ferrari, Elena; Venturelli, M. B.; Sartor, G.; Spisni, Alberto. - In: ITALIAN JOURNAL OF BIOCHEMISTRY. - ISSN 0021-2938. - 53 (3):(2004), pp. 339-339. (Intervento presentato al convegno 49° Congresso Nazionale della Società Italiana di Biochimica e Biologia Molecolare tenutosi a Riccione, Italy nel 28 September -1 October 2004).
File in questo prodotto:
File Dimensione Formato  
rMUP_SIB_2004.pdf

non disponibili

Tipologia: Documento in Post-print
Licenza: NON PUBBLICO - Accesso privato/ristretto
Dimensione 25.63 kB
Formato Adobe PDF
25.63 kB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11381/1443277
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus ND
  • ???jsp.display-item.citation.isi??? ND
social impact