Research Topics
| Maria J MaciasSummaryAffiliation: European Molecular Biology Laboratory Country: Germany Publications
| Collaborators
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Detail Information
Publications
Structural analysis of WW domains and design of a WW prototypeM J Macias
Forschungsinstitut fur Molekulare Pharmakologie, Alfred Kowalke Str 4, 10315 Berlin, Germany
Nat Struct Biol 7:375-9. 2000....
WW and SH3 domains, two different scaffolds to recognize proline-rich ligandsMaria J Macias
Structural and Computational Biology Program, EMBL Heidelberg, Heidelberg, Germany
FEBS Lett 513:30-7. 2002..The binding surface of the modeled WW domain of Npw38 protein shows a remarkable similarity to the SH3 domain of Sem5 protein, confirming biochemical data on similar binding predilections of both domains...
Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40Silke Wiesner
Structural Biology Programme, EMBL Heidelberg, Meyerhofstr 1, 69117 Heidelberg, Germany
J Mol Biol 324:807-22. 2002..In contrast, no interaction was observed between the Prp40 WW domains and the CTD repeats used in this work...
The structure of Prp40 FF1 domain and its interaction with the crn-TPR1 motif of Clf1 gives a new insight into the binding mode of FF domainsAlexander Gasch
Structural Biology Program, EMBL Heidelberg, Meyerhofstrasse 1, 69117 Heidelberg, Germany
J Biol Chem 281:356-64. 2006..Our results also revealed that not all FF domains in Prp40 are functionally equivalent. We proposed that at least two different interaction surfaces exist in FF domains that have evolved to recognize distinct binding motifs...
Structure and dynamics of the human pleckstrin DEP domain: distinct molecular features of a novel DEP domain subfamilyConcepcion Civera
Dpto Quimica Fisica II, Facultad de Farmacia, Universidad Complutense de Madrid, Madrid, Spain
Proteins 58:354-66. 2005..This suggests a role of the pleckstrin DEP domain in intramolecular domain interactions, which is distinct from the functions of other DEP domain subfamilies found so far...
Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domainAlison Z Shaw
ICREA and the Biomedical Research Institute of Barcelona, Barcelona Science Park, Barcelona, Spain
Proteins 60:558-60. 2005
Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW DomainsMarina Brucet
Macrophage Biology Group, Institute for Research in Biomedicine, University of Barcelona, Barcelona, Spain
J Biol Chem 282:14547-57. 2007..Co-immunoprecipitation studies confirmed this interaction with the full-length TREX1 protein, thereby suggesting that TREX1 participates in more functional complexes than previously thought...
Structural characterization of a new binding motif and a novel binding mode in group 2 WW domainsXimena Ramirez-Espain
Institute for Research in Biomedicine Protein NMR group, and the Institució catalana de recerca i estudis avançats ICREA, Barcelona Science Park, Josep Samitier 1 5, E 08028 Barcelona, Spain
J Mol Biol 373:1255-68. 2007..Our results represent the first observation of protein-ligand recognition where a pair of WW and two consecutive motifs in a ligand participate simultaneously...
NMR structural studies of the ItchWW3 domain reveal that phosphorylation at T30 inhibits the interaction with PPxY-containing ligandsBegoña Morales
Institute of Research in Biomedicine, Institucio Catalana de Recerca i Estudis Avancats, Passeig Lluis Companys 23, 08010 Barcelona, Spain
Structure 15:473-83. 2007..This hydrogen-bond formation is precluded in the variant, explaining the inhibition upon phosphorylation. Our results suggest that phosphorylation at position 30 in ItchWW domains can be a mechanism to inhibit target recognition in vivo...
