2cm5
From Proteopedia
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[[Image:2cm5.jpg|left|200px]] | [[Image:2cm5.jpg|left|200px]] | ||
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'''CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN''' | '''CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN''' | ||
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[[Category: Schlicker, C.]] | [[Category: Schlicker, C.]] | ||
[[Category: Sheldrick, G M.]] | [[Category: Sheldrick, G M.]] | ||
| - | [[Category: | + | [[Category: C2 domain]] |
| - | [[Category: | + | [[Category: C2a-c2b linker fragment]] |
| - | [[Category: | + | [[Category: C2b]] |
| - | [[Category: | + | [[Category: Ca2+ binding]] |
| - | [[Category: | + | [[Category: Metal-binding]] |
| - | [[Category: | + | [[Category: Protein transport]] |
| - | [[Category: | + | [[Category: Rabphilin3a]] |
| - | [[Category: | + | [[Category: Synapse]] |
| - | [[Category: | + | [[Category: Synaptic exocytosis]] |
| - | [[Category: | + | [[Category: Transport]] |
| - | [[Category: | + | [[Category: Zinc]] |
| - | [[Category: | + | [[Category: Zinc-finger]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:28:47 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:28, 3 May 2008
CRYSTAL STRUCTURE OF THE C2B DOMAIN OF RABPHILIN
Overview
The Ca(2+) binding properties of C2 domains are essential for the function of their host proteins. We present here the first crystal structures showing an unexpected Ca(2+) binding mode of the C2B domain of rabphilin-3A in atomic detail. Acidic residues from the linker region between the C2A and C2B domains of rabphilin-3A interact with the Ca(2+)-binding region of the C2B domain. Because of these interactions, the coordination sphere of the two bound Ca(2+) ions is almost complete. Mutation of these acidic residues to alanine resulted in a 10-fold decrease in the intrinsic Ca(2+) binding affinity of the C2B domain. Using NMR spectroscopy, we show that this interaction occurred only in the Ca(2+)-bound state of the C2B domain. In addition, this Ca(2+) binding mode was maintained in the C2 domain tandem fragment. In NMR-based liposome binding assays, the linker was not released upon phospholipid binding. Therefore, this unprecedented Ca(2+) binding mode not only shows how a C2 domain increases its intrinsic Ca(2+) affinity, but also provides the structural base for an atypical protein-Ca(2+)-phospholipid binding mode of rabphilin-3A.
About this Structure
2CM5 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
The C2A-C2B linker defines the high affinity Ca(2+) binding mode of rabphilin-3A., Montaville P, Schlicker C, Leonov A, Zweckstetter M, Sheldrick GM, Becker S, J Biol Chem. 2007 Feb 16;282(7):5015-25. Epub 2006 Dec 13. PMID:17166855 Page seeded by OCA on Sat May 3 22:28:47 2008
