MOLECULAR STRUCTURE OF MICROTUBULE-ASSOCIATED PROTEIN 2B AND 2C FROM RAT BRAIN
作者： S Kindler , B Schulz , M Goedert , C C Garner
DOI: 10.1016/S0021-9258(17)45425-1
关键词: Protein secondary structure 、 Protein primary structure 、 Biochemistry 、 Protein domain 、 Binding domain 、 Cell biology 、 Peptide sequence 、 Conserved sequence 、 Domain of unknown function 、 Biology 、 Protein structure
摘要: Full length cDNA clones encoding microtubule-associated proteins (MAP) 2b and 2c from rat brain have been isolated sequenced. The fragments spanning the coding regions for both MAP2b MAP2c were assembled expressed in Escherichia coli. mobility of these bacterial sodium dodecyl sulfate gels is identical to that brain. protein sequence has compared full mouse partial human high molecular weight MAP2. This comparison revealed composed several highly conserved domains flanked by with extensive divergence. Two domains, found either at NH2 or COOH terminus, overlap binding domain regulatory subunit cAMP-dependent kinase II microtubule-binding domain, respectively. A third homologous unknown function lies a central region MAP2b. Secondary structure prediction suggests portion which extends microtubule surface an number alpha-helices separated small turns may account extended yet flexible Interestingly, 4000-base pair deletion middle generates not only removes helices, but also this domain.
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