2giz
From Proteopedia
Structural and functional analysis of Natrin, a member of crisp-3 family blocks a variety of ion channels
Structural highlights
FunctionCRVP1_NAJAT Inhibits calcium-activated potassium channels (KCa1.1/KCNMA1), voltage-gated potassium channel Kv1.3/KCNA3, and the calcium release channel/ryanodine receptor (RyR). Binds specifically to type 1 RyR (RyR1) from skeletal muscle. Inhibit both the binding of ryanodine to RyR1, and RyR1's calcium-channel activity. Inhibits carbachol-induced muscle contraction and weakly blocks muscle contraction evoked by potassium.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our study, crystals of natrin were obtained in two different crystal forms and the structure of one of them was solved at a resolution of 1.68A. Our electrophysiological experiments indicated that natrin can block the ion channel currents of the voltage-gated potassium channel Kv1.3. Docking analyses of the interaction between natrin and Kv1.3 revealed a novel interaction pattern different from the two previously reported K(+) channel inhibition models termed "functional dyad" and "basic ring". These findings offered new insights into the function of natrin and how the specific interactions between CRISPs and different ion channels can be achieved. Structural and functional analysis of natrin, a venom protein that targets various ion channels.,Wang F, Li H, Liu MN, Song H, Han HM, Wang QL, Yin CC, Zhou YC, Qi Z, Shu YY, Lin ZJ, Jiang T Biochem Biophys Res Commun. 2006 Dec 15;351(2):443-8. Epub 2006 Oct 20. PMID:17070778[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
