1f3c: Difference between revisions
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'''REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)''' | {{Structure | ||
|PDB= 1f3c |SIZE=350|CAPTION= <scene name='initialview01'>1f3c</scene> | |||
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'''REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F3C is a [ | 1F3C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. This structure supersedes the now removed PDB entry 1BKQ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F3C OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11178896 11178896] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dynein]] | [[Category: dynein]] | ||
[[Category: light chain]] | [[Category: light chain]] | ||
[[Category: | [[Category: microtubule]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:52 2008'' | ||
Revision as of 09:03, 20 March 2008
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REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)
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
1F3C is a Single protein structure of sequence from Rattus norvegicus. This structure supersedes the now removed PDB entry 1BKQ. 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
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