6qvj: Difference between revisions
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<StructureSection load='6qvj' size='340' side='right'caption='[[6qvj]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='6qvj' size='340' side='right'caption='[[6qvj]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6qvj]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QVJ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6qvj]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QVJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QVJ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TA1:TAXOL'>TA1</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qus|6qus]], [[6quy|6quy]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qus|6qus]], [[6quy|6quy]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAMSAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qvj OCA], [http://pdbe.org/6qvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qvj RCSB], [http://www.ebi.ac.uk/pdbsum/6qvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qvj ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6qvj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qvj OCA], [http://pdbe.org/6qvj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qvj RCSB], [http://www.ebi.ac.uk/pdbsum/6qvj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qvj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CAMP1_HUMAN CAMP1_HUMAN]] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth.<ref>PMID:19508979</ref> <ref>PMID:21834987</ref> <ref>PMID:24117850</ref> [[http://www.uniprot.org/uniprot/TBB5_HUMAN TBB5_HUMAN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [[http://www.uniprot.org/uniprot/TBA1B_HUMAN TBA1B_HUMAN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. | [[http://www.uniprot.org/uniprot/CAMP1_HUMAN CAMP1_HUMAN]] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth.<ref>PMID:19508979</ref> <ref>PMID:21834987</ref> <ref>PMID:24117850</ref> [[http://www.uniprot.org/uniprot/TBB5_HUMAN TBB5_HUMAN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [[http://www.uniprot.org/uniprot/TBA1B_HUMAN TBA1B_HUMAN]] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition. | |||
Structural determinants of microtubule minus end preference in CAMSAP CKK domains.,Atherton J, Luo Y, Xiang S, Yang C, Rai A, Jiang K, Stangier M, Vemu A, Cook AD, Wang S, Roll-Mecak A, Steinmetz MO, Akhmanova A, Baldus M, Moores CA Nat Commun. 2019 Nov 20;10(1):5236. doi: 10.1038/s41467-019-13247-6. PMID:31748546<ref>PMID:31748546</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6qvj" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Akhmanova, A]] | [[Category: Akhmanova, A]] | ||
Revision as of 13:53, 4 December 2019
HsCKK (human CAMSAP1) decorated 14pf taxol-GDP microtubuleHsCKK (human CAMSAP1) decorated 14pf taxol-GDP microtubule
Structural highlights
Function[CAMP1_HUMAN] Probable microtubule-binding protein that plays a role in the regulation of cell morphology and cytoskeletal organization. Through interaction with spectrin may regulate neurite outgrowth.[1] [2] [3] [TBB5_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. [TBA1B_HUMAN] Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Publication Abstract from PubMedCAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition. Structural determinants of microtubule minus end preference in CAMSAP CKK domains.,Atherton J, Luo Y, Xiang S, Yang C, Rai A, Jiang K, Stangier M, Vemu A, Cook AD, Wang S, Roll-Mecak A, Steinmetz MO, Akhmanova A, Baldus M, Moores CA Nat Commun. 2019 Nov 20;10(1):5236. doi: 10.1038/s41467-019-13247-6. PMID:31748546[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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