1mai
From Proteopedia
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| - | [[Image:1mai.gif|left|200px]] | + | [[Image:1mai.gif|left|200px]] |
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| - | '''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE''' | + | {{Structure |
| + | |PDB= 1mai |SIZE=350|CAPTION= <scene name='initialview01'>1mai</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=I3P:D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE'>I3P</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MAI is a [ | + | 1MAI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MAI OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1995 Dec 15;83(6):1037-46. PMID:[http:// | + | Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1995 Dec 15;83(6):1037-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8521504 8521504] |
[[Category: Phosphoinositide phospholipase C]] | [[Category: Phosphoinositide phospholipase C]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
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[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:01 2008'' |
Revision as of 10:41, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN FROM PHOSPHOLIPASE C DELTA IN COMPLEX WITH INOSITOL TRISPHOSPHATE
Overview
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.
About this Structure
1MAI is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain., Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB, Cell. 1995 Dec 15;83(6):1037-46. PMID:8521504
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