Pleckstrin

From Wikipedia, the free encyclopedia

Pleckstrin-1
Ribbon diagram of the C-terminal pleckstrin homology domain of pleckstrin-1 bound to inositol 1,2,3,4,5-pentaphosphate (PDB ID 2I5C)
Identifiers
SymbolPLEK
NCBI gene5341
HGNC9070
OMIM173570
RefSeqNM_002664
UniProtP08567
Other data
LocusChr. 2 p13.3
Search for
StructuresSwiss-model
DomainsInterPro
Pleckstrin-2
Identifiers
SymbolPLEK2
NCBI gene26499
HGNC19238
OMIM608007
PDB1X1G
RefSeqNM_016445
UniProtQ9NYT0
Other data
LocusChr. 14 q23.3q24.1
WikidataQ18038260
Search for
StructuresSwiss-model
DomainsInterPro

Pleckstrins are a family of proteins found in platelets[1] and other cells. The name derives from platelet and leukocyte C kinase substrate and the KSTR string of amino acids. The prototype protein, now called pleckstrin-1, was first identified in 1979 as the major substrate of protein kinase C in platelets.[2] The homolog pleckstrin-2 is more widely expressed in tissues.[3]

The pleckstrin homology domain (PH domain) was named after pleckstrin-1.[2]

Both pleckstrin-1 and pleckstrin-2 contain two pleckstrin homology domains, separated by a central dishevelled-Egl10-pleckstrin (DEP) domain. Pleckstrin-1 is phosphorylated by protein kinase C on three serine and threonine residues located between the first pleckstrin homology domain and the DEP domain;[2] pleckstrin-2 is not a substrate for protein kinase C.[2][4] The two proteins share 65% sequence homology[2] and have a size of about 47 kilodaltons.[5]

As of 2024, no high-resolution three-dimensional structure has been solved for full-length pleckstrin, but the structures of the individual domains of both pleckstrin-1 and -2 have been published.[2]

Functions

References

Related Articles

Wikiwand AI