| Registro completo |
| Provedor de dados: |
Nature Precedings
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| País: |
United Kingdom
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| Título: |
Abundance of intrinsic disorder in SV-IV, a multifunctional androgen-dependent protein secreted from rat seminal vesicle
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| Autores: |
Silvia Vilasi
Raffaele Ragone
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| Data: |
2007-12-06
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| Ano: |
2007
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| Palavras-chave: |
Bioinformatics
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| Resumo: |
The potent immunomodulatory, anti-inflammatory and procoagulant properties of the
protein no. 4 secreted from the rat seminal vesicle epithelium (SV-IV) have been
previously found to be modulated by a supramolecular monomer-trimer equilibrium.
More structural details that integrate experimental data into a predictive framework
have recently been reported. Unfortunately, homology modelling and fold-recognition
strategies were not successful in creating a theoretical model of the structural
organization of SV-IV. It was inferred that the global structure of SV-IV is not similar
to any protein of known three-dimensional structure. Reversing the classical approach
to the sequence-structure-function paradigm, in this paper we report on novel
information obtained by comparing physicochemical parameters of SV-IV with two
datasets made of intrinsically unfolded and ideally globular proteins. In addition, we
have analysed the SV-IV sequence by several publicly available disorder-oriented
predictors. Overall, disorder predictions and a re-examination of existing experimental
data strongly suggest that SV-IV needs large plasticity to efficiently interact with the
different targets that characterize its multifaceted biological function and should be
therefore better classified as an intrinsically disordered protein.
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| Tipo: |
Manuscript
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| Identificador: |
http://precedings.nature.com/documents/1394/version/1
oai:nature.com:10101/npre.2007.1394.1
http://hdl.handle.net/10101/npre.2007.1394.1
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| Fonte: |
Nature Precedings
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| Direitos: |
Creative Commons Attribution 3.0 License
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