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| Hacking Into Cell Communications |
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| SciMed - Biology | |||
| TS-Si News Service | |||
| Friday, 29 January 2010 16:00 | |||
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Hamburg, GER. Scientists have shed new light on cellular communication systems between living cells by hacking into a vital communications system. The discovery increases the possibility of developing new drugs to tackle disorders like neurodegeneration, cancer and cardiovascular disease. Cells rely on a range of signalling systems to communicate with each other and to control their own internal workings. Neurodegeneration is the progressive loss of In a study that appears in Science Signaling, a research team from the the European
London, United Kingdom. New findings argue for the persistence of sex-linked chromosomes, such as the male Y  chromosome, refuting theories that the Y is doomed to extinction.
The results confirm that although these chromosom...Using high-energy X-rays produced by the European Synchrotron Radiation Facility (ESRF) in Grenoble, France, and by the German Synchrotron Radiation Centre (DESY), in Hamburg, Germany, Matthias Wilmanns’ team at EMBL revealed the molecular structure of one of these kinases, a protein called Death-Associated Protein Kinase DAPK, when bound to calmodulin. The structure showed how calmodulin binds to a particular section of DAPK, switching the kinase on so that it can go and change the function of its targets. The team then worked out which of DAPK’s building blocks, or amino acids, were crucial for calmodulin to bind. “Faulty versions of DAPK are involved in the development of some cancers,” says Wilmanns, “so we want to know more about how this protein functions to allow its better exploitation as an anti-cancer target.” What’s more, DAPK has physical similarities to many of the other kinases controlled by calmodulin, meaning many of them are likely to interact with calmodulin in the same, or similar ways. Being able to see the three-dimensional structures of these proteins, how they clip together and alter each other’s behaviour means researchers can devise ways to manipulate this interaction with drugs. “That will provide a platform to get into drug discovery,” says Wilmanns, adding, “obviously, this is the beginning of the story.” He is planning to do so in an ongoing collaboration with Adi Kimchi’s team at the Weizmann Institute in Israel and other groups from EMBL. CitationMolecular Basis of the Death-Associated Protein Kinase–Calcium/Calmodulin Regulator Complex. Iñaki de Diego, Jochen Kuper, Neda Bakalova, Petri Kursula, and Matthias Wilmanns. Science Signaling 2010; 3(106): ra6. doi:10.1126/scisignal.2000552
Abstract Death-associated protein kinase (DAPK) provides a model for calcium-bound calmodulin (CaM)–dependent protein kinases (CaMKs). Here, we report the crystal structure of the binary DAPK-CaM complex, using a construct that includes the DAPK catalytic domain and adjacent autoregulatory domain. When DAPK was in a complex with CaM, the DAPK autoregulatory domain formed a long seven-turn helix. This DAPK-CaM module interacted with the DAPK catalytic domain through two separate domain-domain interfaces, which involved the upper and the lower lobe of the catalytic domain. When bound to DAPK, CaM adopted an extended conformation, which was different from that in CaM-CaMK peptide complexes. Complementary biochemical analysis showed that the ability of DAPK to bind CaM correlated with its catalytic activity. Because many features of CaM binding are conserved in other CaMKs, our findings likely provide a generally applicable model for regulation of CaMK activity.
 The TS-Si News Service is a collaborative effort by TS-Si.org editors, contributors, and corresponding institutions. Sources can include the cited individuals and organizations, as well as TS-Si.org staff contributions. Articles and news reports do not necessarily convey official positions of TS-Si, its partners, or affiliates. We welcome your comments. Use the form below to leave a public comment or send private correspondence via the TS-Si Contact Page. We will not divulge any personal details or place you on a mailing list without your permission.TS-Si is dedicated to the acceptance, medical treatment, and legal protection of individuals correcting the misalignment of their brains and their anatomical sex, while supporting their transition into society as hormonally reconstituted and surgically corrected citizens.
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| Last Updated on Friday, 29 January 2010 17:25 |
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and the TS-Si Research Service are collaborations of TS-Si officials, staff, contributors, and corresponding institutions. The contents do not necessarily convey official positions of TS-Si or its owners, participants, partners, or affiliates.