This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3hkd

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 01:44, 25 December 2014

Tubulin-TN16 : RB3 stathmin-like domain complex

Structural highlights

3hkd is a 5 chain structure with sequence from Ovis aries and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1sa0, 1sa1, 3hkb, 3hkc, 3hke
Gene:	STMN4 (Rattus norvegicus)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[STMN4_RAT] Exhibits microtubule-destabilizing activity.^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Structural changes occur in the alphabeta-tubulin heterodimer during the microtubule assembly/disassembly cycle. Their most prominent feature is a transition from a straight, microtubular structure to a curved structure. There is a broad range of small molecule compounds that disturbs the microtubule cycle, a class of which targets the colchicine-binding site and prevents microtubule assembly. This class includes compounds with very different chemical structures, and it is presently unknown whether they prevent tubulin polymerization by the same mechanism. To address this issue, we have determined the structures of tubulin complexed with a set of such ligands and show that they interfere with several of the movements of tubulin subunits structural elements upon its transition from curved to straight. We also determined the structure of tubulin unliganded at the colchicine site; this reveals that a beta-tubulin loop (termed T7) flips into this site. As with colchicine site ligands, this prevents a helix which is at the interface with alpha-tubulin from stacking onto a beta-tubulin beta sheet as in straight protofilaments. Whereas in the presence of these ligands the interference with microtubule assembly gets frozen, by flipping in and out the beta-subunit T7 loop participates in a reversible way in the resistance to straightening that opposes microtubule assembly. Our results suggest that it thereby contributes to microtubule dynamic instability.

Variations in the colchicine-binding domain provide insight into the structural switch of tubulin.,Dorleans A, Gigant B, Ravelli RB, Mailliet P, Mikol V, Knossow M Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13775-9. Epub 2009 Aug 5. PMID:19666559^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nakao C, Itoh TJ, Hotani H, Mori N. Modulation of the stathmin-like microtubule destabilizing activity of RB3, a neuron-specific member of the SCG10 family, by its N-terminal domain. J Biol Chem. 2004 May 28;279(22):23014-21. Epub 2004 Mar 22. PMID:15039434 doi:http://dx.doi.org/10.1074/jbc.M313693200
↑ Gavet O, El Messari S, Ozon S, Sobel A. Regulation and subcellular localization of the microtubule-destabilizing stathmin family phosphoproteins in cortical neurons. J Neurosci Res. 2002 Jun 1;68(5):535-50. PMID:12111843 doi:http://dx.doi.org/10.1002/jnr.10234
↑ Ravelli RB, Gigant B, Curmi PA, Jourdain I, Lachkar S, Sobel A, Knossow M. Insight into tubulin regulation from a complex with colchicine and a stathmin-like domain. Nature. 2004 Mar 11;428(6979):198-202. PMID:15014504 doi:http://dx.doi.org/10.1038/nature02393
↑ Dorleans A, Gigant B, Ravelli RB, Mailliet P, Mikol V, Knossow M. Variations in the colchicine-binding domain provide insight into the structural switch of tubulin. Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13775-9. Epub 2009 Aug 5. PMID:19666559

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3hkd"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3hkd]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HKD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HKD FirstGlance]. <br>
-</td></tr><tr><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=N16:(3Z,5S)-5-BENZYL-3-[1-(PHENYLAMINO)ETHYLIDENE]PYRROLIDINE-2,4-DIONE'>N16</scene><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=N16:(3Z,5S)-5-BENZYL-3-[1-(PHENYLAMINO)ETHYLIDENE]PYRROLIDINE-2,4-DIONE'>N16</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sa0|1sa0]], [[1sa1|1sa1]], [[3hkb|3hkb]], [[3hkc|3hkc]], [[3hke|3hke]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sa0|1sa0]], [[1sa1|1sa1]], [[3hkb|3hkb]], [[3hkc|3hkc]], [[3hke|3hke]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STMN4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">STMN4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hkd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hkd RCSB], [http://www.ebi.ac.uk/pdbsum/3hkd PDBsum]</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=3hkd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hkd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hkd RCSB], [http://www.ebi.ac.uk/pdbsum/3hkd PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/STMN4_RAT STMN4_RAT]] Exhibits microtubule-destabilizing activity.<ref>PMID:15039434</ref> <ref>PMID:12111843</ref> <ref>PMID:15014504</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 37: @@
 [[Category: Ovis aries]]
 [[Category: Rattus norvegicus]]
-[[Category: Dorleans, A.]]
+[[Category: Dorleans, A]]
-[[Category: Gigant, B.]]
+[[Category: Gigant, B]]
-[[Category: Knossow, M.]]
+[[Category: Knossow, M]]
-[[Category: Mailliet, P.]]
+[[Category: Mailliet, P]]
-[[Category: Mikol, V.]]
+[[Category: Mikol, V]]
-[[Category: Ravelli, R B.G.]]
+[[Category: Ravelli, R B.G]]
 [[Category: Alpha-tubulin]]
 [[Category: Beta-tubulin]]

3hkd

From Proteopedia

Revision as of 01:44, 25 December 2014

Tubulin-TN16 : RB3 stathmin-like domain complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox