Ankyrin repeat domain-containing protein: Difference between revisions

Revision as of 17:53, 27 October 2020

Function

Ankyrin repeat domain-containing protein (ARDCP) recruits kinesin to the cell cortex in order to control microtubule growth via its ankyrin domain^[1].

Disease

Mutations in ARDCP 3 manifest as Bartsocas-Papas syndrome, a genetic disorder characterized by severe craniofacial and limb abnormalities^[2].

Structural highlights

The 3D structure of the complex between human ARDCP 25 C-terminal and a kinesin peptide shows 2 types of interactions. Kinesin residues and residues ^[1]. .

Human ARDCP 25 (cyan and green) complex with kinesin peptide (pink and yellow), sulfate and glycerol (PDB code 5ybv).

Drag the structure with the mouse to rotate

3D structures of ankyrin repeat domain-containing protein3D structures of ankyrin repeat domain-containing protein

4nl9 - hARDCP 3 SAM domain + hARDCP 14 SAM domain - human
5ybj - hARDCP 15 residues 1080-1329
5ybu - hARDCP 15 residues 1080-1329 + KIF21A peptide
4hbd - hARDCP 25 residues 578-832
5ybv - hARDCP 25 residues 578-832 + KIF21A peptide
4cym - hARDCP 27 residues 450-640 + RAB32
4cz2 - hARDCP 27 residues 450-640 + RAB32 + GPPCP
4b93 - hARDCP 27 residues 659-921 + VAMP7
5wni - mARDCP 3 residues 1-342 - mouse
5wnk - mARDCP 3 residues 1-342 (mutant)
5wnj, 5wnm - mARDCP 3 residues 1-342 (mutant) + cancer drug
5wnl - mARDCP 3 residues 1-342 (mutant) + staurosporine
6nxf - mARDCP 31 C-terminal + REC114
5eid, 4tum - AtARDCP 2 residues 211-342 - Arabidopis thaliana
6jd6 - AtARDCP EMB56 + ARDCP

ReferencesReferences

↑ ^1.0 ^1.1 Guo Q, Liao S, Zhu Z, Li Y, Li F, Xu C. Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins. J Biol Chem. 2017 Nov 28. pii: M117.817494. doi: 10.1074/jbc.M117.817494. PMID:29183992 doi:http://dx.doi.org/10.1074/jbc.M117.817494
↑ Huang CS, Oberbeck N, Hsiao YC, Liu P, Johnson AR, Dixit VM, Hymowitz SG. Crystal Structure of Ripk4 Reveals Dimerization-Dependent Kinase Activity. Structure. 2018 May 1;26(5):767-777.e5. doi: 10.1016/j.str.2018.04.002. Epub 2018, Apr 26. PMID:29706531 doi:http://dx.doi.org/10.1016/j.str.2018.04.002

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

[Guo-1] 1.0 ^1.1 Guo Q, Liao S, Zhu Z, Li Y, Li F, Xu C. Structural basis for the recognition of kinesin family member 21A (KIF21A) by the ankyrin domains of KANK1 and KANK2 proteins. J Biol Chem. 2017 Nov 28. pii: M117.817494. doi: 10.1074/jbc.M117.817494. PMID:29183992 doi:http://dx.doi.org/10.1074/jbc.M117.817494

[2] Huang CS, Oberbeck N, Hsiao YC, Liu P, Johnson AR, Dixit VM, Hymowitz SG. Crystal Structure of Ripk4 Reveals Dimerization-Dependent Kinase Activity. Structure. 2018 May 1;26(5):767-777.e5. doi: 10.1016/j.str.2018.04.002. Epub 2018, Apr 26. PMID:29706531 doi:http://dx.doi.org/10.1016/j.str.2018.04.002

[1]

[2]

@@ Line 11: / Line 11: @@
 == Structural highlights ==
-The 3D structure of the complex between human ARDCP 25 C-terminal and a kinesin peptide shows 2 types of interactions.  Kinesin residues <scene name='86/863150/Cv/3'>KARR interact in an acidic pocket</scene> and residues <scene name='86/863150/Cv/4'>QMELLYA interact in a hydrophobic pocket</scene><ref name="Guo"/>. <scene name='86/863150/Cv/5'>Whole kinesin peptide binding site</scene>.
+The 3D structure of the complex between human ARDCP 25 C-terminal and a kinesin peptide shows 2 types of interactions.  Kinesin residues <scene name='86/863150/Cv/3'>KARR interact in an acidic pocket</scene> and residues <scene name='86/863150/Cv/6'>QMELLYA interact in a hydrophobic pocket</scene><ref name="Guo"/>. <scene name='86/863150/Cv/5'>Whole kinesin peptide binding site</scene>.
 </StructureSection>