MLP
From Proteopedia
| Line 1: | Line 1: | ||
| - | Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies. | + | Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called '''Muscle LIM protein''' (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies. |
[[ref]] | [[ref]] | ||
| - | <Structure load='2o10' size='200' frame='true' align='right' caption=' | + | <Structure load='2o10' size='200' frame='true' align='right' caption='NMR structure of human muscle LIM protein 3 with Zn+2 ions, [[2o10]]' scene='Insert optional scene name here' /> |
Revision as of 12:19, 7 August 2012
Three members of Cysteine rich proteins (CRPs) have been identified in vertebrates. CRP3 is localized in Z and M-lines in striated muscles and also called Muscle LIM protein (MLP). All three proteins are associated with the actin cytoskeleton and play similar functions in different muscle varieties. CRPs 1-3 contain 192-194 residues and consist of two LIM domains with the adjacent flexible glycine reach linker region. Each LIM domain comprises two Zn-binding motifs CCHC and CCCC and represents structural and presumably functional independent unit. LIM domains have been intensively characterized using NMR. The solution structures exist for human MLP and other vertebrate CRPs family members. The interactions of MLP with α-actinin, telethonin (T-Cap), βI-spectrin, N-RAP (Nebulin-related-anchoring protein) and cofilin2 (CFL2) have been shown, suggesting its essential role as a scaffold protein in the sarcomere. Potential role of MLP in myogenesis has been reported through the complex formation with muscle helix-loop-helix transcription factors MyoD, MRF4 and myogenin. The mutations of MLP are found in cardiac myopathies. ref
|
