2hkn: Difference between revisions

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==Overview==

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.

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.

==Disease==

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[[Category: Single protein]]

[[Category: Honnappa, S.]]

[[Category: Steinmetz, M.O.]]

[[Category: Steinmetz, M O.]]

[[Category: Winkler, F.K.]]

[[Category: Winkler, F K.]]

[[Category: cytoskeleton associated protein]]

[[Category: eb1 and clip-170 binding protein]]

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[[Category: strand swap]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:51 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==Disease==
@@ Line 17: / Line 17: @@
 [[Category: Single protein]]
 [[Category: Honnappa, S.]]
-[[Category: Steinmetz, M.O.]]
+[[Category: Steinmetz, M O.]]
-[[Category: Winkler, F.K.]]
+[[Category: Winkler, F K.]]
 [[Category: cytoskeleton associated protein]]
 [[Category: eb1 and clip-170 binding protein]]
@@ Line 25: / Line 25: @@
 [[Category: strand swap]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:32:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:51 2008''