G3DSA:1.20.80.10

G3DSA:1.20.80.10

CATH-Gene3D entry
Member databaseCATH-Gene3D
CATH-Gene3D typehomologous superfamily

Description
Imported from IPR014352

This superfamily represents a structural domain with a core structure consisting of a 3-helical closed bundle with a left-handed twist, in an up-and-down arrangement. This structural motif occurs as subdomain 2 within FERM domains, as well as in acyl-CoA-binding proteins. The FERM domain (band F ezrin-radixin-moesin homology domains) has such a structure, acting as a common membrane-binding module involved in localising proteins to the plasma membrane
[1]
. Proteins containing FERM include cytoskeletal proteins such as erythrocyte membrane protein 4.1R, talin, and the ezrin-radixin-moesin protein family, as well as several protein tyrosine kinases and phosphatases, and the neurofibromatosis 2 tumour suppressor protein merlin. The ezrin-radixin-moesin protein family function is to crosslink the actin filaments of cytoskeletal structures to the plasma membrane.

In addition, acyl-CoA-binding protein (ACBP) contains a domain with a similar 3-helical bundle structure. ACBP plays an important role in fatty acid metabolism, maintaining a pool of fatty acyl-CoA molecules in the cell
[2]
.

References
Imported from IPR014352

1.Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Pearson MA, Reczek D, Bretscher A, Karplus PA. Cell 101, 259-70, (2000). View articlePMID: 10847681

2.Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein. van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA. J. Mol. Biol. 309, 181-92, (2001). View articlePMID: 11491287

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