Microtubule-associated protein

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== Structural highlights ==
== Structural highlights ==
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LC3 recognizes a sequestosome peptide which is a preferred target for autophagy and binds at the surface of LC3<ref>PMID:18524774</ref>.
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<scene name='70/708075/Cv/3'>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 shown as red spheres.
</StructureSection>
</StructureSection>

Revision as of 07:57, 10 May 2016

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

Drag the structure with the mouse to rotate

3D Structures of microtubule-associated protein

Updated on 10-May-2016

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. 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
  5. 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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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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