1f95
From Proteopedia
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'''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX''' | '''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX''' | ||
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[[Category: Zhang, M.]] | [[Category: Zhang, M.]] | ||
[[Category: Zhang, Q.]] | [[Category: Zhang, Q.]] | ||
| - | [[Category: | + | [[Category: Bim]] |
| - | [[Category: | + | [[Category: Dlc8]] |
| - | [[Category: | + | [[Category: Dynein]] |
| - | [[Category: | + | [[Category: Light chain]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:03:16 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 13:03, 2 May 2008
SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
Overview
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 Structure
1F95 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Fri May 2 16:03:16 2008
Categories: Protein complex | Rattus norvegicus | Fan, J S. | Li, M. | Tochio, H. | Zhang, M. | Zhang, Q. | Bim | Dlc8 | Dynein | Light chain
