2hkq: Difference between revisions

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-[[Image:2hkq.jpg|left|200px]]
- {{Structure
+==Crystal structure of the C-terminal domain of human EB1 in complex with the CAP-Gly domain of human Dynactin-1 (p150-Glued)==
-|PDB= 2hkq |SIZE=350|CAPTION= <scene name='initialview01'>2hkq</scene>, resolution 1.86&Aring;
+<StructureSection load='2hkq' size='340' side='right'caption='[[2hkq]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[2hkq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HKQ FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86&#8491;</td></tr>
-|GENE= MAPRE1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), DCTN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkq OCA], [https://pdbe.org/2hkq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hkq RCSB], [https://www.ebi.ac.uk/pdbsum/2hkq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hkq ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1txq|1TXQ]], [[2hkn|2HKN]], [[2hl3|2HL3]], [[2hl5|2HL5]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hkq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hkq OCA], [http://www.ebi.ac.uk/pdbsum/2hkq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hkq RCSB]</span>
+[https://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref>
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hk/2hkq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hkq ConSurf].
+<div style="clear:both"></div>
-'''Crystal structure of the C-terminal domain of human EB1 in complex with the CAP-Gly domain of human Dynactin-1 (p150-Glued)'''
+==See Also==
+*[[Dynactin|Dynactin]]
+*[[End-binding protein|End-binding protein]]
-==Overview==
+*[[Microtubule-associated protein 3D structures|Microtubule-associated protein 3D structures]]
-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.
+== References ==
+<references/>
-==Disease==
+__TOC__
-Known disease associated with this structure: Neuropathy, distal hereditary motor, type VIIB OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601143 601143]], Amyotrophic lateral sclerosis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=601143 601143]]
+</StructureSection>
-==About this Structure==
-HKQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HKQ 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:[http://www.ncbi.nlm.nih.gov/pubmed/16949363 16949363]
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Honnappa, S.]]
+[[Category: Honnappa S]]
-[[Category: Steinmetz, M O.]]
+[[Category: Steinmetz MO]]
-[[Category: Winkler, F K.]]
+[[Category: Winkler FK]]
-[[Category: +tip protein complex structure]]
-[[Category: coiled coil]]
-[[Category: cytoskeleton associated protein]]
-[[Category: dynactin]]
-[[Category: eb1]]
-[[Category: microtubule binding]]
-[[Category: p150glued]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:31:45 2008''