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
free
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
free free
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve Pubget Overpricing |
lüll Protein-protein interactions in the membrane: sequence, structural, and biological motifs Moore DT; Berger BW; DeGrado WFStructure 2008[Jul]; 16 (7): 991-1001Single-span transmembrane (TM) helices have structural and functional roles well beyond serving as mere anchors to tether water-soluble domains in the vicinity of the membrane. They frequently direct the assembly of protein complexes and mediate signal transduction in ways analogous to small modular domains in water-soluble proteins. This review highlights different sequence and structural motifs that direct TM assembly and discusses their roles in diverse biological processes. We believe that TM interactions are potential therapeutic targets, as evidenced by natural proteins that modulate other TM interactions and recent developments in the design of TM-targeting peptides.|Amino Acid Motifs[MESH]|Amino Acid Sequence[MESH]|Genetic Diseases, Inborn/genetics[MESH]|Humans[MESH]|Membrane Proteins/*chemistry/genetics/physiology[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Mutation[MESH]|Protein Interaction Domains and Motifs[MESH]|Receptors, Immunologic/chemistry[MESH] |