2hl5: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2hl5.gif|left|200px]]
{{Seed}}
[[Image:2hl5.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hl5|  PDB=2hl5  |  SCENE=  }}  
{{STRUCTURE_2hl5|  PDB=2hl5  |  SCENE=  }}  


'''Crystal structure of the C-terminal domain of human EB1 in complex with the A49M mutant CAP-Gly domain of human Dynactin-1 (p150-Glued)'''
===Crystal structure of the C-terminal domain of human EB1 in complex with the A49M mutant CAP-Gly domain of human Dynactin-1 (p150-Glued)===




==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.
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.
-->
{{ABSTRACT_PUBMED_16949363}}


==Disease==
==Disease==
Line 35: Line 39:
[[Category: Microtubule binding]]
[[Category: Microtubule binding]]
[[Category: P150glued]]
[[Category: P150glued]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:25:08 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:27:29 2008''

Revision as of 16:27, 27 July 2008

File:2hl5.png

Template:STRUCTURE 2hl5

Crystal structure of the C-terminal domain of human EB1 in complex with the A49M mutant CAP-Gly domain of human Dynactin-1 (p150-Glued)

Template:ABSTRACT PUBMED 16949363

Disease

Known disease associated with this structure: Neuropathy, distal hereditary motor, type VIIB OMIM:[601143], Amyotrophic lateral sclerosis, susceptibility to OMIM:[601143]

About this Structure

2HL5 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Key interaction modes of dynamic +TIP networks., Honnappa S, Okhrimenko O, Jaussi R, Jawhari H, Jelesarov I, Winkler FK, Steinmetz MO, Mol Cell. 2006 Sep 1;23(5):663-71. PMID:16949363

Page seeded by OCA on Sun Jul 27 19:27:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2hl5&oldid=663089"