Ankyrin

From Proteopedia

(Difference between revisions)

Revision as of 10:41, 6 March 2019

Human ankyrin-1 ankyrin repeat region (containing 12 repeats) complex with Cl- (green) and Br- (dark red) ions 1n11

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1 Function
2 Disease
3 Relevance
4 Structural highlights
5 3D Structures of ankyrin

Function

Ankyrins (ANK) are proteins which mediate the attachment of membrane proteins to the membrane skeleton. ANKRD2 belongs to the conserved muscle ankyrin repeat protein (MARP) family.Also known as Arpp or stretch responsive muscle ANKRD2 gene contains 9 exons and spans about 12 kb. The 5-prime flanking region contains a TATA box and binding motifs for the muscle-specific transcription factors MYOD and for NF-kappa-B. Kemp et.al cloned mouse Ankrd2 and obtained a partial human ANKRD2 cDNA. Northern blot and PCR analyses detected expression of mouse Ankrd2 only in tissues containing striated muscle. In situ hybridization of mouse embryos showed that Ankrd2 expression was restricted to the myotome of somites at day 9.5. At later developmental stages, Ankrd2 expression was stronger in outer back muscles than intercostal muscles, and it was not expressed in heart. See also

In mammals ANK is encoded by 3 genes: ANK1, ANK2 and ANK3.

ANK1 or ankyrin-R is found in erythrocytes, brain and muscle.
ANK2 or ankyrin-B is found in brain and muscle.
ANK3 or ankyrin-G is found in the nervous system and associates with Na channels.

Gankyrin (GANK) is an oncoprotein which is a component of the 19S cap of the proteasome. GANK contains ankyrin repeats.

Disease

Mutations in erythrocyte ANK1 are associated with spherocytosis. Mutations in ANK2 are associated with cardiac arrhythmia syndrome. Mutations in ANK3 are associated with bipolar disorder.

Relevance

GANK is overexpressed in hepatocellular carcinoma.

Structural highlights

Ankyrin contains four domains: the N terminal which contains 24 ankyrin repeats, a spectrin-binding domain, a death domain which binds to proteins involved in apoptosis and a C terminal regulatory domain. The full-length 328-amino acid mouse protein contains an ATP/GTP-binding domain in its N-terminal half and an ankyrin repeat region in its C-terminal half. It also has a nuclear localization signal, 2 protein-destabilizing PEST sequences, and 2 phosphorylation sites. The ankyrin repeat is a protein-protein interaction motif. It is a 33 residue segment consisting of a helix-loop-helix motif. The long ankyrin repeat in human ankyrin-R contains 12 ankyrin repeats (residues 402-827) and is called D34 region. . ^[1] from 1n0r. ^[2]

3D Structures of ankyrin

Ankyrin 3D structures

References

↑ Michaely P, Tomchick DR, Machius M, Anderson RG. Crystal structure of a 12 ANK repeat stack from human ankyrinR. EMBO J. 2002 Dec 2;21(23):6387-96. PMID:12456646
↑ Mosavi LK, Minor DL Jr, Peng ZY. Consensus-derived structural determinants of the ankyrin repeat motif. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):16029-34. Epub 2002 Dec 2. PMID:12461176 doi:http://dx.doi.org/10.1073/pnas.252537899

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Narendra Kumar Verma

Retrieved from "http://52.214.119.220/wiki/index.php/Ankyrin"

Category: Topic Page

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 </StructureSection>
-== 3D Structures of ankyrin ==
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*Ankyrin
-**[[3so8]] – hANK-1 residues 149-310 - human<br />
-**[[1n11]] – hANK-1 D34 region 402-827<br />
-**[[2yqf]], [[2yvi]] – hANK-1 death domain 1394-1497 – NMR<br />
-**[[3f59]] – hANK-1 spectrin-binding domain 911-1068<br />
-**[[3ud1]], [[3ud2]] - hANK-1 zu5a-zu5b domains 911-1233<br />
-**[[4d8o]] - hANK-1 zu5a-zu5b-upa-dd domains 966-1535<br />
-**[[4rlv]] - hANK-1 + hANK-2<br />
-**[[5y4d]] - hANK-1/hANK-2<br />
-**[[5y4e]] - hANK-2 residues 264-483, 857-896<br />
-**[[5y4f]] - hANK-2 residues 430-873<br />
-**[[4o6x]] - hANK-3 death domain<br />
-**[[1n0q]], [[1n0r]], [[2bkg]], [[2qyj]] – dANK repeats – designed<br />
-**[[2aja]] – LpANK – ''Legionella pneumophila''<br />
-**[[5k34]] – LpANK-2 <br />
-**[[3hra]] – ANK – ''Enterococus faecalis''<br />
-**[[4tum]] – ANK-2 - ''Arabidopsis thaliana'' <br />
-*Ankyrin complexes
-**[[3kbt]], [[3kbu]] - hANK-1 spectrin-binding domain + spectrin β chain<br />
-**[[4qqi]] - hANK-2 + RFX7<br />
-**[[4lg6]] - hANK-2 + CCDC-8<br />
-**[[1svx]] – dANK + maltose-binding protein<br />
-**[[3noc]], [[3nog]] – dANK + acriflavine resistance protein B<br />
-**[[5k35]] – LpANK-2 + SKP1<br />
-**[[4zhb]] – LpANK-2 N-terminal + peptide<br />
-**[[3q9u]], [[3q9n]] – ANK + COA-binding protein – ''Escherichia coli''<br />
-*Gankyrin
-**[[1uoh]], [[1qym]] – hGANK<br />
-**[[1tr4]] – hGANK – NMR<br />
-**[[2dvw]], [[2dwz]], [[3aji]] – GANK + 26S protease regulatory subunit 6B C terminal - mouse
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]

Ankyrin

From Proteopedia

Revision as of 10:41, 6 March 2019

Contents

Function

Disease

Relevance

Structural highlights

3D Structures of ankyrin

References

Proteopedia Page Contributors and Editors (what is this?)

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