1f96
SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
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OverviewOverview
Dyneins are multi-subunit molecular motors that translocate molecular, cargoes along microtubules. Other than acting as an essential component of, the dynein motor complex, the 89-residue subunit of dynein light chain, (DLC8) also regulates a number of other biological events by binding to, various proteins and enzymes. Currently known DLC8 targets include, neuronal nitric oxide synthase; the proapoptotic Bcl-2 family member, protein designated Bim; a Drosophila RNA localization protein Swallow, myosin V, neuronal scaffolding protein GKAP, and IkappaBalpha, an, inhibitor of the NFkappaB transcription factor. The DLC8-binding domains, of the various targets are confined within a short, continuous stretch of, amino acid residues. However, these domains do not share any obvious, sequence homology with each other. Here, the three-dimensional structures, of DLC8 complexed with two peptides corresponding to the DLC8-binding, domains of neuronal nitric oxide synthase and Bim, respectively, were, determined by NMR spectroscopy. Although the two DLC8-binding peptides, have entirely different amino acid sequences, both peptides bind to the, protein with a remarkable similar conformation by engaging the symmetric, DLC8 dimer through antiparallel beta-sheet augmentation via the beta2, strand of the protein. Structural comparison indicates that the two target, peptides use different regions within the conformational flexible, peptide-binding channels to achieve binding specificity. We have also, re-determined the apo-form solution structure of DLC8 in this work. The, structures of the DLC8/target peptide complexes, together with the dynamic, properties of the protein, provide a molecular basis of DLC8's diverse, amino acid sequence-dependent target recognition.
About this StructureAbout this Structure
1F96 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain., Fan J, Zhang Q, Tochio H, Li M, Zhang M, J Mol Biol. 2001 Feb 9;306(1):97-108. PMID:11178896
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