Parvin: Difference between revisions
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Alpha-parvin's structure can be divided into four regions: 1) N-terminal flexible domain (residues 1-96), 2) N-terminal [[CH domain]] (97-200 according to SMART<ref>PMID: 9600884</ref>), 3) linker region (201-241) and 4) C-terminal [[CH domain]] (242-372 identified by limited [[subtilisin]] proteolysis<ref>PMID: 18940607</ref>). Most interactions of alpha-parvin are mapped to the C-terminal CH domain, but CdGAP and perhaps alphaPIX or other, yet unknown partners, interact with the N-terminal flexibile domain. This flexible domain seems to lack a well defined 3D structure and can therefore be classified as a putative [[Intrinsically Disordered Protein|intrinsically disordered]] region. The interactions of this regions with the binding partners are therefore likely to be characterized by relatively low affinity, but high affinity nonetheless.<ref>PMID: 19265676</ref> The abovementioned phosphorylation sites (serines 4 and 8) involved in focal adhesion regulation are located in this segment, which makes them so called disorder-enhanced phosphorylation sites.<ref>PMID: 14960716</ref><ref>PMID: 18388127</ref> | Alpha-parvin's structure can be divided into four regions: 1) N-terminal flexible domain (residues 1-96), 2) N-terminal [[CH domain]] (97-200 according to SMART<ref>PMID: 9600884</ref>), 3) linker region (201-241) and 4) C-terminal [[CH domain]] (242-372 identified by limited [[subtilisin]] proteolysis<ref>PMID: 18940607</ref>). Most interactions of alpha-parvin are mapped to the C-terminal CH domain, but CdGAP and perhaps alphaPIX or other, yet unknown partners, interact with the N-terminal flexibile domain. This flexible domain seems to lack a well defined 3D structure and can therefore be classified as a putative [[Intrinsically Disordered Protein|intrinsically disordered]] region. The interactions of this regions with the binding partners are therefore likely to be characterized by relatively low affinity, but high affinity nonetheless.<ref>PMID: 19265676</ref> The abovementioned phosphorylation sites (serines 4 and 8) involved in focal adhesion regulation are located in this segment, which makes them so called disorder-enhanced phosphorylation sites.<ref>PMID: 14960716</ref><ref>PMID: 18388127</ref> | ||
<Structure load='2vzc' scene='User:Marcin_Jozef_Suskiewicz/Sandbox_Parvin//Parvin/1' size=' | <Structure load='2vzc' scene='User:Marcin_Jozef_Suskiewicz/Sandbox_Parvin//Parvin/1' size='300' frame='true' align='left' caption='Structure of the C-terminal CH domain of alpha-parvin(PDB entry [[2vzc]])'/> | ||
===C-terminal CH domain=== | ===C-terminal CH domain=== | ||
The [[CH domain|calponin-homology (CH) domains]] are helical structural units around 100 amino acids long. They comprise at least four helices, three of them forming a helical bundle. CH domains usually comprise elements of big multidomain proteins and are present either in singlet<ref>PMID: 19459066</ref> or duplex/tandem arrangement.<ref>PMID: 19565353</ref> The tandem arrangement of CH domains is often associated with F-actin binding<ref>PMID: 9708889</ref><ref>PMID: 18952167</ref> (and is thus called actin-binding domain or ABD), but generally CH domains seem to be characterized by functional plasticity and ability to bind various structural motifs.<ref>PMID: 11911887</ref> In the case of alpha-parvin, the interactions of CH domains with both F-actin and other partners (paxillin, ILK) are observed. The interactions with paxillin and ILK are mediated by a single CH domain, the C-terminal one. This domain has attracted most attention. While no full-length structure of alpha-parvin has been solved to date, the structure of the C-terminal CH domain, on its own<ref>PMID: 18940607</ref> and in complexes (with paxillin<ref>PMID: 18940607</ref><ref>PMID: 18508764</ref> and the pseudokinase domain of ILK<ref>PMID: 20005845</ref>) are available. | The [[CH domain|calponin-homology (CH) domains]] are helical structural units around 100 amino acids long. They comprise at least four helices, three of them forming a helical bundle. CH domains usually comprise elements of big multidomain proteins and are present either in singlet<ref>PMID: 19459066</ref> or duplex/tandem arrangement.<ref>PMID: 19565353</ref> The tandem arrangement of CH domains is often associated with F-actin binding<ref>PMID: 9708889</ref><ref>PMID: 18952167</ref> (and is thus called actin-binding domain or ABD), but generally CH domains seem to be characterized by functional plasticity and ability to bind various structural motifs.<ref>PMID: 11911887</ref> In the case of alpha-parvin, the interactions of CH domains with both F-actin and other partners (paxillin, ILK) are observed. The interactions with paxillin and ILK are mediated by a single CH domain, the C-terminal one. This domain has attracted most attention. While no full-length structure of alpha-parvin has been solved to date, the structure of the C-terminal CH domain, on its own<ref>PMID: 18940607</ref> and in complexes (with paxillin<ref>PMID: 18940607</ref><ref>PMID: 18508764</ref> and the pseudokinase domain of ILK<ref>PMID: 20005845</ref>) are available. | ||