1mup

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1mup, resolution 2.4Å

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PHEROMONE BINDING TO TWO RODENT URINARY PROTEINS REVEALED BY X-RAY CRYSTALLOGRAPHY

Overview

The principal protein excreted in male rat urine, urinary alpha 2-globulin and the homologous mouse protein, major urinary protein, have been well characterized, although their functions remain unclear. Male rat urine affects the behaviour and sexual response of female rats, leading to the proposal that rodent urinary proteins are responsible for binding pheromones and their subsequent release from drying urine. Urinary alpha 2-globulin is also involved in hyaline droplet nephropathy, an important toxicological syndrome in male rats resulting from exposure to a number of industrial chemicals and characterized by the accumulation of liganded urinary alpha 2-globulin in lysosomes in the kidney, followed by the induction of renal cancer. We now report the three-dimensional structures of mouse major urinary protein (at 2.4 A resolution) and rat urinary alpha 2-globulin (at 2.8 A resolution). The results corroborate the role of these proteins in pheromone transport and elaborate the structural basis of ligand binding.

About this Structure

1MUP is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography., Bocskei Z, Groom CR, Flower DR, Wright CE, Phillips SE, Cavaggioni A, Findlay JB, North AC, Nature. 1992 Nov 12;360(6400):186-8. PMID:1279439

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