کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1932591 1536788 2009 6 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
The binding cavity of mouse major urinary protein is optimised for a variety of ligand binding modes
چکیده انگلیسی

15N and 1HN chemical shift data and 15N relaxation studies have been used to characterise the binding of N-phenyl-naphthylamine (NPN) to mouse major urinary protein (MUP). NPN binds in the β-barrel cavity of MUP, hydrogen bonding to Tyr120 and making extensive non-bonded contacts with hydrophobic side chains. In contrast to the natural pheromone 2-sec-butyl-4,5-dihydrothiazole, NPN binding gives no change to the overall mobility of the protein backbone of MUP. Comparison with 11 different ligands that bind to MUP shows a range of binding modes involving 16 different residues in the β-barrel cavity. These finding justify why MUP is able to adapt to allow for many successful binding partners.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 390, Issue 4, 25 December 2009, Pages 1266–1271
نویسندگان
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