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Cited by 603

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain

Open access
Ferguson, Kathryn M., Lemmon, Mark A., Schlessinger, Joseph, Sigler, Paul B.·1995·Cell
DOI 10.1016/0092-8674(95)90219-8
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Abstract

The X-ray crystal structure of the high affinity complex between the pleckstrin homology (PH) domain from rat phospholipase C-delta 1 (PLC-delta 1) and inositol-(1,4,5)-trisphosphate (Ins(1,4,5)P3) has been refined to 1.9 A resolution. The domain fold is similar to others of known structure. Ins(1,4,5)P3 binds on the positively charged face of the electrostatically polarized domain, interacting predominantly with the beta 1/beta 2 and beta 3/beta 4 loops. The 4- and 5-phosphate groups of Ins(1,4,5)P3 interact much more extensively than the 1-phosphate. Two amino acids in the PLC-delta 1 PH domain that contact Ins(1,4,5)P3 have counterparts in the Bruton's tyrosine kinase (Btk) PH domain, where mutational changes cause inherited agammaglobulinemia, suggesting a mechanism for loss of function in Btk mutants. Using electrostatics and varying levels of head-group specificity, PH domains may localize and orient signaling proteins, providing a general membrane targeting and regulatory function.

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Metadata

Authors
Ferguson, K. M., Lemmon, M. A., Schlessinger, J., & Sigler, P. B.
Venue
Cell
Publisher
Elsevier BV
Published
1995-12
Volume
83
Issue
6
Pages
1037-1046
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/0092-8674(95)90219-8
OpenAlex
W2092249847
Cited by
603
References
1
FWCI
16.93
Type
journal article
Language
en
Open access
hybrid

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