کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1179576 | 962784 | 2006 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Prediction of the mechanism of action of omuralide (clasto-lactacystin β-lactone) on human cathepsin A based on a structural model of the yeast proteasome β5/PRE2-subunit/omuralide complex
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cathepsin A (CathA) is a lysosomal serine carboxypeptidase that exhibits homology and structural similarity to the yeast and wheat serine carboxypeptidases (CPY and CPW) belonging to the α/β-hydrolase fold family. Human CathA (hCathA) and CPW have been demonstrated to be inhibited by a proteasome (threonine protease) inhibitor, lactacystin, and its active derivative, omuralide (clasto-lactacystin β-lactone), as well as chymostatin. A hCathA/omuralide complex model constructed on the basis of the X-ray crystal structures of the CPW/chymostatin complex and the yeast proteasome β-subunit (β5/PRE2)/omuralide one predicted that the conformation of omuralide in the active-site cleft of proteasome β5/PRE2 should be very similar to that of chymostatin at the S1 catalytic subsites in the hCathA- and CPW-complexes. The relative positions of the glycine residues, i.e., Gly57 in hCathA, Gly53 in CPW, and Gly47 in β5/PRE2, present in the oxyanion hole of each enzyme were also highly conserved. These results suggest that omuralide might inhibit hCathA and CPW at the S1 subsite in their active-site clefts through direct binding to the active serine residue.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1764, Issue 8, August 2006, Pages 1372-1380
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1764, Issue 8, August 2006, Pages 1372-1380
نویسندگان
Sei-ichi Aikawa, Fumiko Matsuzawa, Yurie Satoh, Yoshito Kadota, Hirofumi Doi, Kohji Itoh,