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
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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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
Journal: Biochemical and Biophysical Research Communications - Volume 390, Issue 4, 25 December 2009, Pages 1266–1271
نویسندگان
Thelma A. Pertinhez, Elena Ferrari, Emanuela Casali, Jital A. Patel, Alberto Spisni, Lorna J. Smith,