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| {{STRUCTURE_2hkn| PDB=2hkn | SCENE= }} | | {{STRUCTURE_2hkn| PDB=2hkn | SCENE= }} |
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| '''Crystal structure of the CAP-Gly domain of human Dynactin-1 (p150-Glued)'''
| | ===Crystal structure of the CAP-Gly domain of human Dynactin-1 (p150-Glued)=== |
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| ==Overview==
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| Dynamic microtubule plus-end tracking protein (+TIP) networks are implicated in all functions of microtubules, but the molecular determinants of their interactions are largely unknown. Here, we have explored key binding modes of +TIPs by analyzing the interactions between selected CAP-Gly, EB-like, and carboxy-terminal EEY/F-COO(-) sequence motifs. X-ray crystallography and biophysical binding studies demonstrate that the beta2-beta3 loop of CAP-Gly domains determines EB-like motif binding specificity. They further show how CAP-Gly domains serve as recognition domains for EEY/F-COO(-) motifs, which represent characteristic and functionally important sequence elements in EB, CLIP-170, and alpha-tubulin. Our findings provide a molecular basis for understanding the modular interaction modes between alpha-tubulin, CLIPs, EB proteins, and the dynactin-dynein motor complex and suggest that multiple low-affinity binding sites in different combinations control dynamic +TIP networks at microtubule ends. They further offer insights into the structural consequences of genetic CAP-Gly domain defects found in severe human disorders.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16949363}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16949363 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16949363}} |
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| ==Disease== | | ==Disease== |
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| [[Category: P150-glued]] | | [[Category: P150-glued]] |
| [[Category: Strand swap]] | | [[Category: Strand swap]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:24:11 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:37:09 2008'' |
