2pzo
From Proteopedia
(New page: 200px<br /> <applet load="2pzo" size="450" color="white" frame="true" align="right" spinBox="true" caption="2pzo, resolution 2.60Å" /> '''Crystal structure o...) |
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| - | [[Image:2pzo. | + | [[Image:2pzo.jpg|left|200px]]<br /><applet load="2pzo" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2pzo" size=" | + | |
caption="2pzo, resolution 2.60Å" /> | caption="2pzo, resolution 2.60Å" /> | ||
'''Crystal structure of the zinc-knuckle 2 domain of human CLIP-170 in complex with CAP-Gly domain of human Dynactin-1 (p150-Glued)'''<br /> | '''Crystal structure of the zinc-knuckle 2 domain of human CLIP-170 in complex with CAP-Gly domain of human Dynactin-1 (p150-Glued)'''<br /> | ||
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==Overview== | ==Overview== | ||
In all eukaryotes, CAP-Gly proteins control important cellular processes., The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed, between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle, of CLIP170 as a model system to explore the structure-function, relationship of CAP-Gly-mediated protein interactions. We demonstrate that, the conserved GKNDG motif of CAP-Gly domains is responsible for targeting, to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and, microtubules. The CAP-Gly-EEY/F interaction is essential for the, recruitment of the dynactin complex by CLIP170 and for activation of, CLIP170. Our findings define the molecular basis of CAP-Gly domain, function, including the tubulin detyrosination-tyrosination cycle. They, further establish fundamental roles for the interaction between CAP-Gly, proteins and C-terminal EEY/F sequence motifs in regulating complex and, dynamic cellular processes. | In all eukaryotes, CAP-Gly proteins control important cellular processes., The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed, between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle, of CLIP170 as a model system to explore the structure-function, relationship of CAP-Gly-mediated protein interactions. We demonstrate that, the conserved GKNDG motif of CAP-Gly domains is responsible for targeting, to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and, microtubules. The CAP-Gly-EEY/F interaction is essential for the, recruitment of the dynactin complex by CLIP170 and for activation of, CLIP170. Our findings define the molecular basis of CAP-Gly domain, function, including the tubulin detyrosination-tyrosination cycle. They, further establish fundamental roles for the interaction between CAP-Gly, proteins and C-terminal EEY/F sequence motifs in regulating complex and, dynamic cellular processes. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Amyotrophic lateral sclerosis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601143 601143]], Neuropathy, distal hereditary motor, type VIIB OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601143 601143]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2PZO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2PZO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PZO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-knuckle]] | [[Category: zinc-knuckle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:50:38 2008'' |
Revision as of 10:50, 23 January 2008
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Crystal structure of the zinc-knuckle 2 domain of human CLIP-170 in complex with CAP-Gly domain of human Dynactin-1 (p150-Glued)
Overview
In all eukaryotes, CAP-Gly proteins control important cellular processes., The molecular mechanisms underlying the functions of CAP-Gly domains, however, are still poorly understood. Here we use the complex formed, between the CAP-Gly domain of p150(glued) and the C-terminal zinc knuckle, of CLIP170 as a model system to explore the structure-function, relationship of CAP-Gly-mediated protein interactions. We demonstrate that, the conserved GKNDG motif of CAP-Gly domains is responsible for targeting, to the C-terminal EEY/F sequence motifs of CLIP170, EB proteins and, microtubules. The CAP-Gly-EEY/F interaction is essential for the, recruitment of the dynactin complex by CLIP170 and for activation of, CLIP170. Our findings define the molecular basis of CAP-Gly domain, function, including the tubulin detyrosination-tyrosination cycle. They, further establish fundamental roles for the interaction between CAP-Gly, proteins and C-terminal EEY/F sequence motifs in regulating complex and, dynamic cellular processes.
About this Structure
2PZO is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Structure-function relationship of CAP-Gly domains., Weisbrich A, Honnappa S, Jaussi R, Okhrimenko O, Frey D, Jelesarov I, Akhmanova A, Steinmetz MO, Nat Struct Mol Biol. 2007 Oct;14(10):959-67. Epub 2007 Sep 9. PMID:17828277
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