QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Purchase Article View Shopping Cart Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Wang, Y. Articles by Tajkhorshid, E. Search for Related Content PubMed PubMed Citation Articles by Wang, Y. Articles by Tajkhorshid, E.

---

Supplement: Aromatic Amino Acids and Related Substances: Chemistry, Biology, Medicine, and Application: SESSION 1

Molecular Mechanisms of Conduction and Selectivity in Aquaporin Water Channels^1–3,

Department of Biochemistry, Center for Biophysics and Computational Biology, and Beckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, IL 61801

^* To whom correspondence should be addressed. E-mail: emad{at}life.uiuc.edu.

Aquaporins (AQP) are a family of membrane channels primarily responsible for conducting water across cellular membranes. The availability of a large body of high resolution structural data along with numerous atomic-scale simulation studies have resulted in an unprecedented level of understanding of the mechanism of function and selectivity in AQP. In this article, after summarizing major highlights of structure-functional studies of AQP, we will report on some of our recent large-scale molecular dynamics simulations investigating the mechanisms of permeation of various substances through pure lipid bilayers and through multiple pathways provided by tetrameric structures of different AQP. Comparison of the results obtained for structurally highly homologous, but functionally distinct, AQP allowed us to identify novel mechanisms of gating and selectivity of these channels and to design mutants with experimentally verified, altered properties. When applicable, special attention will be given to specific aromatic amino acids and their involvement in various functional aspects of AQP.

This article has been cited by other articles:

				R. Horsefield, K. Norden, M. Fellert, A. Backmark, S. Tornroth-Horsefield, A. C. Terwisscha van Scheltinga, J. Kvassman, P. Kjellbom, U. Johanson, and R. Neutze High-resolution x-ray structure of human aquaporin 5 PNAS, September 9, 2008; 105(36): 13327 - 13332. [Abstract] [Full Text] [PDF]

				Z. Su, X. Zhou, W. J. Haynes, S. H. Loukin, A. Anishkin, Y. Saimi, and C. Kung Yeast gain-of-function mutations reveal structure function relationships conserved among different subfamilies of transient receptor potential channels PNAS, December 4, 2007; 104(49): 19607 - 19612. [Abstract] [Full Text] [PDF]

				K. Takai Introduction to the Transdisciplinary International Conference on Aromatic Amino Acids and Related Substances: Chemistry, Biology, Medicine, and Application J. Nutr., June 1, 2007; 137(6): 1501S - 1503S. [Full Text] [PDF]