EVH1 domains: structure, function and interactions
نویسندگان
چکیده
منابع مشابه
Diversity of polyproline recognition by EVH1 domains.
Enabled/VASP Homology-1 (EVH1) domains function primarily as interaction modules that link signaling proteins by binding to proline-rich sequences. EVH1 domains are ~115 residues in length and adopt the pleckstrin homology (PH) fold. Four different protein families contain EVH1 domains: Ena/VASP, Homer, WASP and SPRED. Except for the SPRED domains, for which no binding partners are known, EVH1 ...
متن کاملDiscovering Domains Mediating Protein Interactions
Background: Protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. The majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. Most of the former studies focus only on interacting domain pairs. However they do not consider the in...
متن کاملdiscovering domains mediating protein interactions
background: protein-protein interactions do not provide any direct information regarding the domains within the proteins that mediate the interactions. the majority of proteins are multi domain proteins and the interaction between them is often defined by the pairs of their domains. most of the former studies focus only on interacting domain pairs. however they do not consider the interaction...
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In order for cells to respond to their environment, a series of regulated molecular events has to take place. External signalling molecules bind to cellular receptors and thereby trigger the activation of multiple intracellular pathways, which modify cellular phenotypes. The cell-surface receptors for a wide range of polypeptide hormones possess protein tyrosine kinase activity, which is induce...
متن کاملStructure and function of KH domains.
The hnRNP K homology (KH) domain was first identified in the protein human heterogeneous nuclear ribonucleoprotein K (hnRNP K) 14 years ago. Since then, KH domains have been identified as nucleic acid recognition motifs in proteins that perform a wide range of cellular functions. KH domains bind RNA or ssDNA, and are found in proteins associated with transcriptional and translational regulation...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2001
ISSN: 0014-5793
DOI: 10.1016/s0014-5793(01)03291-4