2v5m: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2v5m.jpg|left|200px]] | [[Image:2v5m.jpg|left|200px]] | ||
'''STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY''' | {{Structure | ||
|PDB= 2v5m |SIZE=350|CAPTION= <scene name='initialview01'>2v5m</scene>, resolution 1.95Å | |||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |||
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2V5M is a [ | 2V5M 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=2V5M OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis of Dscam isoform specificity., Meijers R, Puettmann-Holgado R, Skiniotis G, Liu JH, Walz T, Wang JH, Schmucker D, Nature. 2007 Sep 27;449(7161):487-91. Epub 2007 Aug 26. PMID:[http:// | Structural basis of Dscam isoform specificity., Meijers R, Puettmann-Holgado R, Skiniotis G, Liu JH, Walz T, Wang JH, Schmucker D, Nature. 2007 Sep 27;449(7161):487-91. Epub 2007 Aug 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17721508 17721508] | ||
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 37: | ||
[[Category: neurobiology spl]] | [[Category: neurobiology spl]] | ||
''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 18:43:13 2008'' | ||
Revision as of 19:43, 20 March 2008
| |||||||
| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS FOR DSCAM ISOFORM SPECIFICITY
OverviewOverview
The Dscam gene gives rise to thousands of diverse cell surface receptors thought to provide homophilic and heterophilic recognition specificity for neuronal wiring and immune responses. Mutually exclusive splicing allows for the generation of sequence variability in three immunoglobulin ecto-domains, D2, D3 and D7. We report X-ray structures of the amino-terminal four immunoglobulin domains (D1-D4) of two distinct Dscam isoforms. The structures reveal a horseshoe configuration, with variable residues of D2 and D3 constituting two independent surface epitopes on either side of the receptor. Both isoforms engage in homo-dimerization coupling variable domain D2 with D2, and D3 with D3. These interactions involve symmetric, antiparallel pairing of identical peptide segments from epitope I that are unique to each isoform. Structure-guided mutagenesis and swapping of peptide segments confirm that epitope I, but not epitope II, confers homophilic binding specificity of full-length Dscam receptors. Phylogenetic analysis shows strong selection of matching peptide sequences only for epitope I. We propose that peptide complementarity of variable residues in epitope I of Dscam is essential for homophilic binding specificity.
About this StructureAbout this Structure
2V5M is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of Dscam isoform specificity., Meijers R, Puettmann-Holgado R, Skiniotis G, Liu JH, Walz T, Wang JH, Schmucker D, Nature. 2007 Sep 27;449(7161):487-91. Epub 2007 Aug 26. PMID:17721508
Page seeded by OCA on Thu Mar 20 18:43:13 2008