Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
 
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve
Pubget Overpricing |  
lüll
Functional plasticity of CH domains Gimona M; Djinovic-Carugo K; Kranewitter WJ; Winder SJFEBS Lett 2002[Feb]; 513 (1): 98-106With the refinement of algorithms for the identification of distinct motifs from sequence databases, especially those using secondary structure predictions, new protein modules have been determined in recent years. Calponin homology (CH) domains were identified in a variety of proteins ranging from actin cross-linking to signaling and have been proposed to function either as autonomous actin binding motifs or serve a regulatory function. Despite the overall structural conservation of the unique CH domain fold, the individual modules display a quite striking functional variability. Analysis of the actopaxin/parvin protein family suggests the existence of novel (type 4 and type 5) CH domain families which require special attention, as they appear to be a good example for how CH domains may function as scaffolds for other functional motifs of different properties.|Actinin/chemistry/metabolism[MESH]|Amino Acid Sequence[MESH]|Animals[MESH]|Binding Sites[MESH]|Calcium-Binding Proteins/chemistry/*metabolism[MESH]|Calponins[MESH]|Dictyostelium/physiology[MESH]|Microfilament Proteins[MESH]|Molecular Sequence Data[MESH]|Muscle Proteins/chemistry/metabolism[MESH]|Protein Binding[MESH]|Protein Structure, Secondary[MESH]|Sequence Alignment[MESH]|Sequence Homology, Amino Acid[MESH]|Spectrin/*chemistry/metabolism[MESH] |
