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dc.creatorWallnoefer, Hannes G.es_ES
dc.creatorLingott, Torstenes_ES
dc.creatorGutiérrez, José Maríaes_ES
dc.creatorMerfort, Irmgardes_ES
dc.creatorLiedl, Klaus R.es_ES
dc.date.accessioned2016-11-28T20:35:06Zes_ES
dc.date.available2016-11-28T20:35:06Zes_ES
dc.date.issued2010-07-09es_ES
dc.identifier.citationhttp://pubs.acs.org/doi/abs/10.1021/ja909908yes_ES
dc.identifier.issn0002-7863es_ES
dc.identifier.urihttp://hdl.handle.net/10669/29325es_ES
dc.description.abstractProtein-protein interfaces have crucial functions in many biological processes. The large interaction areas of such interfaces show complex interaction motifs. Even more challenging is the understanding of (multi)specificity in protein-protein binding. Many proteins can bind several partners to mediate their function. A perfect paradigm to study such multispecific protein-protein interfaces are snake venom metalloproteases (SVMPs). Inherently, they bind to a variety of basement membrane proteins of capillaries, hydrolyze them, and induce profuse bleeding. However, despite having a high sequence homology, some SVMPs show a strong hemorrhagic activity, while others are (almost) inactive. We present computer simulations indicating that the activity to induce hemorrhage, and thus the capability to bind the potential reaction partners, is related to the backbone flexibility in a certain surface region. A subtle interplay between flexibility and rigidity of two loops seems to be the prerequisite for the proteins to carry out their damaging function. Presumably, a significant alteration in the backbone dynamics makes the difference between SVMPs that induce hemorrhage and the inactive ones.es_ES
dc.language.isoen_USes_ES
dc.sourceJournal of the America Chemical Society; Volumen 132, Número 30. 2010es_ES
dc.subjectAmino acid sequencees_ES
dc.subjectAnimalses_ES
dc.subjectCrystallography, X-Rayes_ES
dc.subjectMetalloproteaseses_ES
dc.subjectMolecular dynamics simulationes_ES
dc.subjectMolecular sequence dataes_ES
dc.subjectProtein bindinges_ES
dc.subjectProtein conformationes_ES
dc.subjectSequence alignmentes_ES
dc.subjectSnakees_ES
dc.subjectSnake venomes_ES
dc.titleBackbone Flexibility Controls the Activity and Specificity of a Protein−Protein Interface: Specificity in Snake Venom Metalloproteaseses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.typeArtículo científicoes_ES
dc.identifier.doi10.1021/ja909908yes_ES
dc.description.procedenceUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)es_ES


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