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| | {{STRUCTURE_1dro| PDB=1dro | SCENE= }} | | {{STRUCTURE_1dro| PDB=1dro | SCENE= }} |
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| - | '''NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN'''
| + | ===NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN=== |
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| - | ==Overview==
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| - | BACKGROUND: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. RESULTS: We have solved the solution structure of the 122-residue PH domain of Drosophila beta-spectrin. The overall fold consists of two antiparallel beta-sheets packing against each other at an angle of approximately 60 degrees to form a beta-sandwich, a two-turn alpha-helix unique to spectrin PH domains, and a four-turn C-terminal alpha-helix. One of the major insertions in beta-spectrin PH domains forms a long, basic surface loop and appears to undergo slow conformational exchange in solution. This loop shows big spectral changes upon addition of D-myo-inositol 1,4,5-trisphosphate (IP3). CONCLUSIONS: We propose that the groove at the outer surface of the second beta-sheet is an important site of association with other proteins. This site and the possible lipid-binding site can serve to localize the spectrin network under the plasma membrane. More generally, it has to be considered that the common fold observed for the PH domain structures solved so far does not necessarily mean that all PH domains have similar functions. In fact, the residues constituting potential binding sites for ligands or other proteins are only slightly conserved between different PH domains.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8591029}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8591029 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8591029}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1DRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. | + | 1DRO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRO OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Zhang, P.]] | | [[Category: Zhang, P.]] |
| | [[Category: Cytoskeleton]] | | [[Category: Cytoskeleton]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:11:38 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:30:59 2008'' |
Revision as of 20:31, 30 June 2008
Template:STRUCTURE 1dro
NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN
Template:ABSTRACT PUBMED 8591029
About this Structure
1DRO is a Single protein structure of sequence from Drosophila melanogaster. Full experimental information is available from OCA.
Reference
Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin., Zhang P, Talluri S, Deng H, Branton D, Wagner G, Structure. 1995 Nov 15;3(11):1185-95. PMID:8591029
Page seeded by OCA on Mon Jun 30 23:30:59 2008
