1xa6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1xa6.gif|left|200px]] | [[Image:1xa6.gif|left|200px]] | ||
'''Crystal Structure of the Human Beta2-Chimaerin''' | {{Structure | ||
|PDB= 1xa6 |SIZE=350|CAPTION= <scene name='initialview01'>1xa6</scene>, resolution 3.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure of the Human Beta2-Chimaerin''' | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
1XA6 is a [ | 1XA6 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=1XA6 OCA]. | ||
==Reference== | ==Reference== | ||
Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin., Canagarajah B, Leskow FC, Ho JY, Mischak H, Saidi LF, Kazanietz MG, Hurley JH, Cell. 2004 Oct 29;119(3):407-18. PMID:[http:// | Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin., Canagarajah B, Leskow FC, Ho JY, Mischak H, Saidi LF, Kazanietz MG, Hurley JH, Cell. 2004 Oct 29;119(3):407-18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15507211 15507211] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 28: | Line 37: | ||
[[Category: racgap]] | [[Category: racgap]] | ||
''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 15:07:07 2008'' | ||
Revision as of 16:07, 20 March 2008
| |||||||
| , resolution 3.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of the Human Beta2-Chimaerin
OverviewOverview
The lipid second messenger diacylglycerol acts by binding to the C1 domains of target proteins, which translocate to cell membranes and are allosterically activated. Here we report the crystal structure at 3.2 A resolution of one such protein, beta2-chimaerin, a GTPase-activating protein for the small GTPase Rac, in its inactive conformation. The structure shows that in the inactive state, the N terminus of beta2-chimaerin protrudes into the active site of the RacGAP domain, sterically blocking Rac binding. The diacylglycerol and phospholipid membrane binding site on the C1 domain is buried by contacts with the four different regions of beta2-chimaerin: the N terminus, SH2 domain, RacGAP domain, and the linker between the SH2 and C1 domains. Phospholipid binding to the C1 domain triggers the cooperative dissociation of these interactions, allowing the N terminus to move out of the active site and thereby activating the enzyme.
DiseaseDisease
Known disease associated with this structure: Apnea, postanesthetic OMIM:[177400]
About this StructureAbout this Structure
1XA6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin., Canagarajah B, Leskow FC, Ho JY, Mischak H, Saidi LF, Kazanietz MG, Hurley JH, Cell. 2004 Oct 29;119(3):407-18. PMID:15507211
Page seeded by OCA on Thu Mar 20 15:07:07 2008