3
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Book Chapter: not found
      Peptides: The Wave of the Future 

      The Role of Unstructured Highly Charged Regions on the Stability and Specificity of Dimerization of Two-Stranded α-Helical Coiled-Coils: Neck Region of Kinesin-Like Motor Protein Kif3A

      other

      , ,

      Springer Netherlands

      Read this book at

      Buy book Bookmark
          There is no author summary for this book yet. Authors can add summaries to their books on ScienceOpen to make them more accessible to a non-specialist audience.

          Related collections

          Most cited references 2

          • Record: found
          • Abstract: found
          • Article: not found

          The design plan of kinesin motors.

          The kinesin superfamily comprises a large and structurally diverse group of microtubule-based motor proteins that produce a variety of force-generating activities within cells. This review addresses how the structures of kinesin proteins provide clues as to their biological functions and motile properties. We discuss structural features common to all kinesin motors, as well as specialized features that enable subfamilies of related motors to carry out specialized activities. We also discuss how the kinesin motor domain uses chemical energy from ATP hydrolysis to move along microtubules.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Heterodimerization of the two motor subunits of the heterotrimeric kinesin, KRP85/95.

            The heterotrimeric kinesin-related motor protein, KRP85/95 is assembled from two kinesin-related polypeptides, SpKRP85 and SpKRP95, together with an uncharacterized 115 kDa polypeptide. Here we report the deduced amino acid sequence of SpKRP95, a close relative of SpKRP85. Both SpKRP85 and SpKRP95 are predicted to have a tripartite domain organization consisting of an N-terminal motor domain, a central stalk domain capable of coiled-coil formation, and a second globular C-terminal domain. The sequences of the central stalk domains predict that SpKRP85 and SpKRP95 should be capable of forming heterodimeric coiled coils. Furthermore, SpKRP85-SpKRP95 complexes can be immunoprecipitated from a cell-free translation system, providing direct evidence that SpKRP85 and SpKRP95 are capable of heterodimerization.
              Bookmark

              Author and book information

              Book
              978-94-010-3905-5
              978-94-010-0464-0
              2001
              10.1007/978-94-010-0464-0
              Book Chapter
              2001
              : 359-360
              10.1007/978-94-010-0464-0_165

              Comments

              Comment on this book

              Book chapters

              Similar content 1,351