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Group:MUZIC:Myopalladin

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Revision as of 11:22, 13 July 2011

Contents

Introduction

NMR structure of the domain Ig1 of human Palladin

Drag the structure with the mouse to rotate



Domains and Interactions

Ig domains and their binding partners

Image:Myopalladin-Palladin.png
Modular organisation of Myopalladin and Palladin

Myopalladin comprises 5 Ig domains separated by inserted sequences for which no structural domains could be predicted from the sequence. The only structural data related to Myopalladin are the NMR structures of Ig domain 1 (PDB code 2DM2 [[1]]) and Ig domain 2 (PDB code 2DM3 [[2]]) of Palladin (homologous to Ig domains 3 and 4 of Myopalladin, respectively).

CARP

The N-terminal region of Myopalaldin, going from the N-terminal end to the domain Ig2, was shown to interact with the full length CARP.

Alpha-Actinin

The C-terminal region of Myopalaldin, going from the domain Ig3 to the very C-terminal end, was shown to interact with the EF-hand region of Alpha-Actinin.

Inserted sequences and their binding partners

Myopalladin Ig domains are separated by 6 Inserted Sequences (IS). The IS3 comprises a Proline-rich region that has been shown to interact with the SH3 domain of Nebulin and Nebulette.

References

  1. Bang ML, Mudry RE, McElhinny AS, Trombitas K, Geach AJ, Yamasaki R, Sorimachi H, Granzier H, Gregorio CC, Labeit S. Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles in Z-disc and I-band protein assemblies. J Cell Biol. 2001 Apr 16;153(2):413-27. PMID:11309420

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Marie-Cecile Pelissier, Nikos Pinotsis, Michal Harel

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