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1f96
From Proteopedia
(New page: 200px<br /><applet load="1f96" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f96" /> '''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (...) |
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| - | [[Image:1f96.gif|left|200px]]<br /><applet load="1f96" size=" | + | [[Image:1f96.gif|left|200px]]<br /><applet load="1f96" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f96" /> | caption="1f96" /> | ||
'''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX'''<br /> | '''SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Dyneins are multi-subunit molecular motors that translocate molecular | + | 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== | ==About this Structure== | ||
| - | 1F96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1F96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F96 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fan, J | + | [[Category: Fan, J S.]] |
[[Category: Li, M.]] | [[Category: Li, M.]] | ||
[[Category: Tochio, H.]] | [[Category: Tochio, H.]] | ||
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[[Category: nnos]] | [[Category: nnos]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:36:12 2008'' |
Revision as of 10:36, 21 February 2008
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SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS 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
1F96 is a Single protein structure of sequence 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 Thu Feb 21 12:36:12 2008
Categories: Rattus norvegicus | Single protein | Fan, J S. | Li, M. | Tochio, H. | Zhang, M. | Zhang, Q. | Dlc8 | Dynein | Light chain | Nnos
