1pls
From Proteopedia
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| - | [[Image:1pls.gif|left|200px]] | + | [[Image:1pls.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN''' | + | {{Structure |
| + | |PDB= 1pls |SIZE=350|CAPTION= <scene name='initialview01'>1pls</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PLS is a [ | + | 1PLS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PLS OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure of a pleckstrin-homology domain., Yoon HS, Hajduk PJ, Petros AM, Olejniczak ET, Meadows RP, Fesik SW, Nature. 1994 Jun 23;369(6482):672-5. PMID:[http:// | + | Solution structure of a pleckstrin-homology domain., Yoon HS, Hajduk PJ, Petros AM, Olejniczak ET, Meadows RP, Fesik SW, Nature. 1994 Jun 23;369(6482):672-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8208296 8208296] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''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 13:25:59 2008'' |
Revision as of 11:26, 20 March 2008
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| Gene: | CDNA (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN
Contents |
Overview
Pleckstrin, the major protein kinase C substrate of platelets, contains domains of about 100 amino acids at the amino and carboxy termini that have been found in a number of proteins, including serine/threonine kinases, GTPase-activating proteins, phospholipases and cytoskeletal proteins. These conserved sequences, termed pleckstrin-homology (PH) domains, are thought to be involved in signal transduction. But the details of the function and binding partners of the PH domains have not been characterized. Here we report the solution structure of the N-terminal pleckstrin-homology domain of pleckstrin determined using heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. The structure consists of an up-and-down beta-barrel of seven antiparallel beta-strands and a C-terminal amphiphilic alpha-helix that caps one end of the barrel. The overall topology of the domain is similar to that of the retinol-binding protein family of structures.
Disease
Known disease associated with this structure: Age-related maculopathy, susceptibility to OMIM:[607772]
About this Structure
1PLS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of a pleckstrin-homology domain., Yoon HS, Hajduk PJ, Petros AM, Olejniczak ET, Meadows RP, Fesik SW, Nature. 1994 Jun 23;369(6482):672-5. PMID:8208296
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