High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: The formin homology 1 domain of mDial and the proline-rich domain of VASP

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作者： Kursula P ^[1] ; Kursula I ^[2] ; Massimi M ^[3] ; Song YH ; Downer J ; Stanley WA ; Witke W ; Wilmanns M

作者单位： EMBL Hamburg Outstn, DESY, D-22607 Hamburg, Germany ^[1] EMBL Monterotondo Outstn, Monterotondo, Italy ^[2] Univ Oulu, Dept Biochem, Oulu, Finland ^[3]

关键词 profilin actin crystal structure mDia1 VASP POLY-L-PROLINE FORMIN HOMOLOGY-2 DOMAIN ACTIN-BINDING PROTEIN F-ACTIN ACANTHAMOEBA PROFILIN ENA/VASP PROTEINS LISTERIA-MONOCYTOGENES FH2 DOMAIN MACROMOLECULAR STRUCTURES INTRACELLULAR MOTILITY

发布时间 2013-11-20

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Journal of Molecular Biology

2008年375卷1期

270-290页

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High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: The formin homology 1 domain of mDial and the proline-rich domain of VASP

Journal of Molecular Biology

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Journal of Molecular Biology

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High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: The formin homology 1 domain of mDial and the proline-rich domain of VASP

Journal of Molecular Biology

相似文献

Journal of Molecular Biology

相关期刊

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