چاپ صفحه |  صفحه نخست سامانه |  چکیده مقاله |  نویسندگان |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده ثبت کننده مقاله | سیاوش دستمالچی |
| مرحله جاری مقاله | مقالات چاپ شده سامانه قبلی |
| دانشکده/مرکز مربوطه | دانشگاه علوم پزشکی تبریز |
| کد مقاله | 10073 |
| عنوان فارسی مقاله | Comparison of the transmembrane helices of bovine rhodopsin in the crystal structure and the C template based on cryo-electron microscopy maps and sequence analysis of the G protein-coupled receptors |
| عنوان لاتین مقاله | Comparison of the transmembrane helices of bovine rhodopsin in the crystal structure and the Cα template based on cryo-electron microscopy maps and sequence analysis of the G protein-coupled receptors |
| ناشر | 5 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ | بلی |
| عنوان نشریه (خارج از لیست فوق) | Molecular Simulation |
| نوع مقاله | Original Article |
| نحوه ایندکس شدن مقاله | ایندکس شده سطح یک – ISI - Web of Science |
| آدرس لینک مقاله/ همایش در شبکه اینترنت | http://www.ingentaconnect.com/content/tandf/gmos/2002/00000028/00000008/art00009 |
| G protein-coupled receptors (GPCR) are activated by a diverse array of extracellular signals, ranging from light to polypeptide molecules. The receptors propagate these signals intracellularly using G protein secondary messenger pathways. A common feature in the architecture of these receptors is their seven transmembrane domains. The first crystal structure of a GPCR, bovine rhodopsin, has recently been solved at 2.8 Å. We compared the seven membrane-spanning helices (TMH) from the crystal structure of bovine rhodopsin with those from the low-resolution model of bovine rhodopsin based on the cryo-electron microscopy structure of frog rhodopsin developed by Dr Joyce Baldwin. The model developed by Baldwin used a consensus sequence approach to predict the rotational position of each helix with respect to the other six helices. Superposition of the entire helix bundle of the Baldwin model with the crystal structure gave a RMS difference (RMSD) of 3.2 Å for the 198 C α atoms which suggests a high level of similarity in the arrangement of the helices. Except for TMH IV (RMSD of 4.0 Å), the position of corresponding helices within the helix bundle overlapped well. The superposition of individual helices showed that the RMSD values over 3 Å in the global superposition were largely due to one or more of the following: (i) differences in the unraveling and kinks for these helices, (ii) translation of TMH perpendicular to the membrane and (iii) rotation of helices up to 31 °, except for TMH IV in which an additional contribution to the RMSD came from the aforementioned observation. As other crystal structures of GPCRs become available, a comparison with the Baldwin consensus model may reveal larger differences than those observed here. © 2002 Taylor & Francis Ltd. |
| نویسنده | نفر چندم مقاله |
|---|---|
| سیاوش دستمالچی | اول |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| dastmalchi2002.pdf | 1395/08/26 | 142864 | دانلود |
