By I Barry Holland,Susan P. C. Cole,Karl Kuchler, et al.Elsevier|Elsevier Science||Academic PressAdult NonfictionScienceLanguage(s): EnglishOn sale date: 13.10.2011Street date: 07.01.2003
ABC Proteins is an in-depth, up to date research of all that's identified concerning the topic thus far. It discusses and compares evolution, biology and mechanism of motion of all recognized ABC proteins, together with the 1st structural reviews in addition to medical implications. will probably be valuable to a person attempting to remain abreast of the newest findings. This booklet is certain to turn into a vintage and should on a regular basis be updated.
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Extra info for ABC Proteins. From Bacteria to Man
In contrast, bacterial species that occupy a more restricted growth niche (for example, mammalian pathogenic species) have far fewer ABC transporters. Eukaryotic cells generally have fewer ABC transporters, presumably because other more sophisticated mechanisms for moving solutes across membranes have evolved. For example, cells which can absorb nutrients by endocytosis do not require ABC transporters for the uptake of nutrients, although ABC transporters still play an important role in the uptake of solutes into organelles (Almashanu and Valle, Chapter 24; Lill and Kispal, Chapter 25).
Class 3 contains all known BPD transporters and systems with ill-characterized function or transport mechanism, some of the latter being considered as exporters. This classification is indeed useful for predicting the putative functions of open reading frames (ORFs) of unknown function based on primary sequence similarities. This concept is justified by the fact that proteins or protein domains that participate in similar functions are found in the same phylogenetic cluster. 3B showing the different dispositions of the highly conserved but functionally different MDR1, MDR3 and BSEP proteins).
1985;4:1033–1040. , et al. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature. 1986;323:448–450. , Ferro-Luzzi Ames G. ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system. Proc. Natl Acad. Sci. USA. 1984;81:7333–7337. F. Structural and functional relationships of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport. Nature. 1990;346:362–365. F. The ABC (ATP-binding cassette) transporters of Escherichia coli.