1zm0
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= PLEK, P47 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= PLEK, P47 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1xxo|1XXO]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zm0 OCA], [http://www.ebi.ac.uk/pdbsum/1zm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zm0 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed. | Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed. | ||
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| - | ==Disease== | ||
| - | Known disease associated with this structure: Age-related maculopathy, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=607772 607772]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: pleckstrin]] | [[Category: pleckstrin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:38:35 2008'' |
Revision as of 22:38, 30 March 2008
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| , resolution 2.100Å | |||||||
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| Gene: | PLEK, P47 (Homo sapiens) | ||||||
| Related: | 1XXO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Carboxyl Terminal PH Domain of Pleckstrin To 2.1 Angstroms
Overview
Pleckstrin is an important intracellular protein involved in the phosphoinositide-signalling pathways of platelet activation. This protein contains both N- and C-terminal pleckstrin-homology (PH) domains (N-PH and C-PH). The crystal structure of C-PH was solved by molecular replacement and refined at 2.1 Angstroms resolution. Two molecules were observed within the asymmetric unit and it is proposed that the resulting dimer interface could contribute to the previously observed oligomerization of pleckstrin in resting platelets. Structural comparisons between the phosphoinositide-binding loops of the C-PH crystal structure and the PH domains of DAPP1 and TAPP1, the N-terminal PH domain of pleckstrin and a recently described solution structure of C-PH are presented and discussed.
About this Structure
1ZM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the carboxy-terminal PH domain of pleckstrin at 2.1 Angstroms., Jackson SG, Zhang Y, Bao X, Zhang K, Summerfield R, Haslam RJ, Junop MS, Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):324-30. Epub 2006, Feb 22. PMID:16510979
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