This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| Line 1: | Line 1: | ||
| - | [[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 /> | ||
| Line 6: | Line 5: | ||
==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. | ||
| - | |||
| - | ==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== | ||
| Line 31: | Line 27: | ||
[[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
|
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
Page seeded by OCA on Wed Jan 23 12:50:38 2008
