Microtubule-associated protein

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== Structural highlights ==
== Structural highlights ==
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<scene name='70/708075/Cv/4'>LC3 recognizes a sequestosome peptide which is a preferred target for autophagy and binds at the surface of LC3</scene><ref>PMID:18524774</ref>. Water molecules are shown as red spheres.
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<scene name='70/708075/Cv/5'>LC3 recognizes a sequestosome peptide which is a preferred target for autophagy and binds at the surface of LC3</scene><ref>PMID:18524774</ref>. Water molecules are shown as red spheres.
== 3D Structures of microtubule-associated protein ==
== 3D Structures of microtubule-associated protein ==
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</StructureSection>
</StructureSection>
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== 3D Structures of microtubule-associated protein ==
 
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
 
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{{#tree:id=OrganizedByTopic|openlevels=0|
 
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*MAP
 
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**[[6fc5]] – MAP CAP-Gly domain – yeast<br /><br />
 
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*MAP1 light chain 3A
 
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**[[1ugm]], [[3eci]], [[3wal]], [[4zdv]]– hLC3A – human<br />
 
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**[[3wan]] – hLC3A/ATG13 LIR<br />
 
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**[[5dpr]], [[5dpw]] – hLC3A/PLEKHM1 LIR<br />
 
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**[[5cx3]], [[5d94]] – hLC3A + FYC01 LIR<br />
 
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*MAP1 light chain 3B
 
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**[[3vtu]], [[5xac]] – hLC3B<br />
 
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**[[1v49]] – hLC3B – NMR<br />
 
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**[[3vtv]], [[3vtw]] – hLC3B/optineurin (mutant)<br />
 
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**[[3wao]] – hLC3B/ATG13 LIR<br />
 
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**[[3x0w]] – hLC3B/PLEKHM1 LIR<br />
 
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**[[4waa]] – hLC3B/NIX LIR<br />
 
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**[[5ms6]], [[5xae]] – hLC3B/RAVZ LIR<br />
 
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**[[5v4k]] – hLC3B/NEDD4 LIR<br />
 
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**[[5dcn]] – hLC3B + TECPR2 LIR<br />
 
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**[[2lue]] – hLC3B + optineurin peptide<br />
 
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**[[2zjd]] – hLC3B + sequestosome p62 peptide<br />
 
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**[[5xad]] – hLC3B + peptide<br />
 
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**[[229x]], [[5gmv]] – hLC3B + FUNDC1 peptide<br />
 
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**[[5ms2]], [[5ms5]] – hLC3B + RAVZ<br />
 
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**[[5w9a]] – hLC3B + Trim5a<br />
 
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**[[2z0d]], [[2z0e]], [[2zzp]] – rLC3B + hCysteine protease ATG4B – rat<br />
 
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**[[2k6q]] – rLC3B + sequestosome p62 peptide - NMR<br />
 
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**[[5wrd]] – LC3B + FYVE peptide - mouse<br />
 
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**[[5yis]], [[5yiq]] – mLC3B + ankyrin peptide <br />
 
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*MAP1 light chain 3C
 
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**[[3wam]] – hLC3C<br />
 
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**[[2ncn]] – hLC3C - NMR<br />
 
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**[[3vvw]] – hLC3C + NDP52<br />
 
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**[[3w1y]] – hLC3C + ribosomal protein S10<br />
 
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**[[3wap]] – hLC3C/ATG13 LIR<br />
 
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**[[4eoy]] – LC3C (mutant) + ATG3 – ''Plasmodium falciparum''<br />
 
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*Microtubule-associated protein tau
 
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**[[6hre]], [[6hrf]], [[6nwp]], [[6nwq]] – hTau residues 1-441 – Cryo EM<br />
 
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**[[6qjq]] – hTau residues 196-289 – Cryo EM<br />
 
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**[[6qjh]], [[6qjm]], [[6qjp]], [[6qjq]] – hTau residues 272-330 – Cryo EM<br />
 
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**[[2mz7]] – hTau residues 584-629 - NMR<br />
 
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**[[5o3t]], [[5o3o]], [[5o3l]] – hTau residues 623-695 – Cryo EM<br />
 
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**[[5n5b]] – hTau residues 292-319 - NMR<br />
 
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**[[1i8h]] – hTau peptide + PIN1 WW domain - NMR<br />
 
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**[[2on9]], [[4e0n]], [[4e0o]], [[4e0m]], [[4np8]] – hTau peptide <br />
 
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**[[3ovl]] – hTau peptide + Orange G<br />
 
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**[[4glr]], [[4tqe]], [[5dmg]] – hTau peptide + antibody<br />
 
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**[[4fl5]], [[4y32]], [[4y3b]], [[4y5i]] – hTau peptide + 14-3-3 protein σ<br />
 
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**[[6cvn]], [[6cvj]] – hTau residues 198-399 + tubulin<br />
 
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*Microtubule-associated protein RP/EB family member 1
 
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**[[1wu9]] – hMAPRE1 C-terminal<br />
 
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**[[1yib]], [[1yig]] – hMAPRE1 C-terminal dimerization domain<br />
 
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**[[1vka]], [[2r8u]], [[1pa7]], [[1ueg]] – hMAPRE1 N-terminal<br />
 
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**[[2qjz]] – hMAPRE1 CH domain <br />
 
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**[[3gjo]] – hMAPRE1 C-terminal + dystonin peptide<br />
 
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**[[1txq]], [[2hkq]], [[2hl5]] – hMAPRE1 C-terminal + dynactin CAP-Gly domain<br />
 
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**[[3tq7]] – hMAPRE1 C-terminal + hRPEB member 3 C-terminal + dynactin CAP-Gly domain<br />
 
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**[[6evi]] – mMAPRE1 C-terminal - NMR<br />
 
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**[[6evq]] – mMAPRE1 C-terminal + tetrazol derivative - NMR<br />
 
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*Microtubule-associated protein RP/EB family member 3
 
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**[[3co1]] – hMAPRE3 CH domain <br />
 
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**[[1wyo]] – hMAPRE3 CH domain - NMR<br />
 
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**[[3jak]], [[3jal]], [[3gar]] – hMAPRE3 CH domain + tubulin + 3GTP – Cryo EM<br />
 
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**[[1v5k]] – mMAPRE3 CH domain - NMR<br />
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human microtubule-associated protein light chain 3B (cyan) complex with sequestosome peptide (green) (PDB code 2zjd)

Drag the structure with the mouse to rotate

References

  1. Maccioni RB, Cambiazo V. Role of microtubule-associated proteins in the control of microtubule assembly. Physiol Rev. 1995 Oct;75(4):835-64. PMID:7480164
  2. Halpain S, Dehmelt L. The MAP1 family of microtubule-associated proteins. Genome Biol. 2006;7(6):224. PMID:16938900
  3. Lebouvier T, Scales TM, Williamson R, Noble W, Duyckaerts C, Hanger DP, Reynolds CH, Anderton BH, Derkinderen P. The microtubule-associated protein tau is also phosphorylated on tyrosine. J Alzheimers Dis. 2009;18(1):1-9. doi: 10.3233/JAD-2009-1116. PMID:19542604 doi:http://dx.doi.org/10.3233/JAD-2009-1116
  4. Buligescu L, Lenkei R, Ciontea M, Dan EM. [Significance of anti-albumin antibodies in chronic liver disease]. Rev Med Interna Neurol Psihiatr Neurochir Dermatovenerol Med Interna. 1977, Jul-Aug;29(4):363-70. PMID:22919
  5. Turtola LO. Enamel microhardness and fluoride uptake underneath fermenting and non-fermenting artificial plaque. Scand J Dent Res. 1977 Sep;85(6):373-9. PMID:22924
  6. Schraen-Maschke S, Dhaenens CM, Delacourte A, Sablonniere B. Microtubule-associated protein tau gene: a risk factor in human neurodegenerative diseases. Neurobiol Dis. 2004 Apr;15(3):449-60. PMID:15056452 doi:http://dx.doi.org/10.1016/j.nbd.2003.12.009
  7. Ichimura Y, Kumanomidou T, Sou YS, Mizushima T, Ezaki J, Ueno T, Kominami E, Yamane T, Tanaka K, Komatsu M. Structural basis for sorting mechanism of p62 in selective autophagy. J Biol Chem. 2008 Aug 15;283(33):22847-57. Epub 2008 Jun 4. PMID:18524774 doi:http://dx.doi.org/M802182200

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