Download PDF by Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric: Aquaporins

By Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric Beitz (eds.)

ISBN-10: 3540798846

ISBN-13: 9783540798842

ISBN-10: 3540798854

ISBN-13: 9783540798859

The aquaporin box has matured at an incredibly quick speed and we're on the verge to improve severe recommendations to therapeutically modulate aquaporin functionality at once or through regulatory networks. Key must haves can be found at the present time: i. a substantial (and starting to be) variety of aquaporin crystal buildings for the rational layout of inhibitory molecules, ii. complex molecular dynamics simulation suggestions for theoretical analyses of selectivity mechanisms and docking experiments, iii. finished facts on aquaporin immunohistochemistry, iv. aquaporin knockout animals for physiological reviews, and v. assay platforms for compound library screenings. The constitution of this quantity on aquaporins follows the issues laid out above and hence covers the advancements from simple examine to strength pharmacological use. positioned among pharmacology textbooks and up to date clinical papers this booklet presents a well timed evaluation for readers from the basic in addition to the utilized disciplines.

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Hepatology 37:1435–1441 Gresz V, Kwon TH, Gong H, Agre P, Steward MC, King LS, Nielsen S (2004) Immunolocalization of AQP-5 in rat parotid and submandibular salivary glands after stimulation or inhibition of secretion in vivo. Am J Physiol Gastrointest Liver Physiol 287:G151–G161 Gu F, Zhai H, Li D, Zhao L, Li C, Huang S, Ma X (2007) A novel mutation in major intrinsic protein of the lens gene (MIP) underlies autosomal dominant cataract in a Chinese family. Mol Vis 13:1651–1656 Hamann S, Zeuthen T, la Cour M, Nagelhus E, Ottersen OP, Agre P, Nielsen S (1998) Aquaporins in complex tissues.

2005), and plant SoPIP2;1 (Tornroth-Horsefield et al. 2006). In the following paragraphs we discuss the basic AQP fold, the structure of the channel, and specific features of the extracellular surfaces of specific AQPs that exhibit an adhesive function. 1 The AQP Fold An AQP monomer is built from six transmembrane helices arranged in a righthanded helical bundle that provides the framework for the channel (Fig. 1b). The angle at which the transmembrane helices are oriented gives rise to funnel-shaped cytoplasmic and extracellular vestibules connected by the conduction pore.

32 33 36 37 38 38 41 45 45 48 49 50 51 51 Abstract Progress in the structure determination of AQPs has led to a deep understanding of water and solute permeation by these small integral membrane proteins. The atomic structures now available have allowed the water permeation and exclusion of protons to be monitored by molecular dynamics simulations, and have provided a framework for assessing the water and solute permeation in great detail by site-directed mutations.

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Aquaporins by Jennifer M. Carbrey, Peter Agre (auth.), Prof. Dr. Eric Beitz (eds.)


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