1F96

SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX

Summary for 1F96

• Entry DOI: 10.2210/pdb1f96/pdb
• Related: 1F3C
• NMR Information: BMRB: 4911
• Descriptor: DYNEIN LIGHT CHAIN 8, PROTEIN (NNOS, NEURONAL NITRIC OXIDE SYNTHASE) (2 entities in total)
• Functional Keywords: dynein, light chain, dlc8, nnos, inhibitor-oxidoreductase complex, inhibitor/oxidoreductase
• Biological source: Rattus norvegicus (Norway rat); More
• Total number of polymer chains: 4
• Total formula weight: 24860.40

Authors

Fan, J.S.,Zhang, Q.,Tochio, H.,Li, M.,Zhang, M. (deposition date: 2000-07-07, release date: 2001-02-28, Last modification date: 2024-05-22)

Primary citation

Fan, J.,Zhang, Q.,Tochio, H.,Li, M.,Zhang, M.
Structural basis of diverse sequence-dependent target recognition by the 8 kDa dynein light chain.
J.Mol.Biol., 306:97-108, 2001

PubMed Abstract: 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.

PubMed: 11178896
DOI: 10.1006/jmbi.2000.4374

Experimental method

SOLUTION NMR