دورية أكاديمية
Bioinformatics of the TULIP domain superfamily.
| العنوان: | Bioinformatics of the TULIP domain superfamily. |
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| المؤلفون: | Kopec KO; Department of Protein Evolution, Max-Planck-Institute for Developmental Biology, Spemannstrasse 35, 72076 Tübingen, Germany., Alva V, Lupas AN |
| المصدر: | Biochemical Society transactions [Biochem Soc Trans] 2011 Aug; Vol. 39 (4), pp. 1033-8. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Review |
| اللغة: | English |
| بيانات الدورية: | Publisher: Portland Press On The Behalf Of The Biochemical Society Country of Publication: England NLM ID: 7506897 Publication Model: Print Cited Medium: Internet ISSN: 1470-8752 (Electronic) Linking ISSN: 03005127 NLM ISO Abbreviation: Biochem Soc Trans Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: London : Portland Press On The Behalf Of The Biochemical Society |
| مواضيع طبية MeSH: | Carrier Proteins/*genetics , Protein Structure, Tertiary/*genetics, Animals ; Cluster Analysis ; Computational Biology ; Evolution, Molecular ; Humans ; Lipids/chemistry ; Sequence Homology, Amino Acid |
| مستخلص: | Proteins of the BPI (bactericidal/permeability-increasing protein)-like family contain either one or two tandem copies of a fold that usually provides a tubular cavity for the binding of lipids. Bioinformatic analyses show that, in addition to its known members, which include BPI, LBP [LPS (lipopolysaccharide)-binding protein)], CETP (cholesteryl ester-transfer protein), PLTP (phospholipid-transfer protein) and PLUNC (palate, lung and nasal epithelium clone) protein, this family also includes other, more divergent groups containing hypothetical proteins from fungi, nematodes and deep-branching unicellular eukaryotes. More distantly, BPI-like proteins are related to a family of arthropod proteins that includes hormone-binding proteins (Takeout-like; previously described to adopt a BPI-like fold), allergens and several groups of uncharacterized proteins. At even greater evolutionary distance, BPI-like proteins are homologous with the SMP (synaptotagmin-like, mitochondrial and lipid-binding protein) domains, which are found in proteins associated with eukaryotic membrane processes. In particular, SMP domain-containing proteins of yeast form the ERMES [ER (endoplasmic reticulum)-mitochondria encounter structure], required for efficient phospholipid exchange between these organelles. This suggests that SMP domains themselves bind lipids and mediate their exchange between heterologous membranes. The most distant group of homologues we detected consists of uncharacterized animal proteins annotated as TM (transmembrane) 24. We propose to group these families together into one superfamily that we term as the TULIP (tubular lipid-binding) domain superfamily. |
| المشرفين على المادة: | 0 (Carrier Proteins) 0 (Lipids) |
| تواريخ الأحداث: | Date Created: 20110727 Date Completed: 20111115 Latest Revision: 20110726 |
| رمز التحديث: | 20231215 |
| DOI: | 10.1042/BST0391033 |
| PMID: | 21787343 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1470-8752 |
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| DOI: | 10.1042/BST0391033 |