Novel structural insights into F-actin-binding and novel functions of calponin homology domains. Export

@article{citeulike:5793928, abstract = {Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alpha-helical leucin-aspartate rich motif from paxillin.}, author = {Sj\"{o}blom, Bj\"{o}rn and Yl\"{a}nne, Jari and Djinovi\'{c}-Carugo, Kristina}, citeulike-article-id = {5793928}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.sbi.2008.10.003}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18952167}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18952167}, doi = {10.1016/j.sbi.2008.10.003}, issn = {1879-033X}, journal = {Current opinion in structural biology}, keywords = {cytoskeletal-dynamics, modular, review}, month = {December}, number = {6}, pages = {702--708}, posted-at = {2009-09-17 04:10:49}, priority = {4}, title = {Novel structural insights into F-actin-binding and novel functions of calponin homology domains.}, url = {http://dx.doi.org/10.1016/j.sbi.2008.10.003}, volume = {18}, year = {2008} }

TY - JOUR ID - citeulike:5793928 L3 - citeulike-article-id:5793928 N2 - Tandem calponin homology (CH) domains are well-known actin filaments (F-actin) binding motifs. There has been a continuous debate about the details of CH domain-actin interaction, mainly because atomic level structures of F-actin are not available. A recent electron microscopy study has considerably advanced our structural understanding of CH domain:F-actin complex. On the contrary, it has recently also been shown that CH domains can bind other macromolecular systems: two CH domains from separate polypeptides Ncd80, Nuf2 can form a microtubule-binding site, as well as tandem CH domains in the EB1 dimer, while the single C-terminal CH domain of alpha-parvin has been observed to bind to a alpha-helical leucin-aspartate rich motif from paxillin. IS - 6 JF - Current opinion in structural biology SN - 1879-033X EP - 708 TI - Novel structural insights into F-actin-binding and novel functions of calponin homology domains. VL - 18 SP - 702 KW - cytoskeletal-dynamics KW - modular KW - review AU - Sjöblom, Björn AU - Ylänne, Jari AU - Djinović-Carugo, Kristina PY - 2008/12// UR - http://dx.doi.org/10.1016/j.sbi.2008.10.003 ER -