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3dow
From Proteopedia
| 3dow, resolution 2.30Å () | |||||||||
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| Gene: | GABARAP, FLC3B (Homo sapiens) | ||||||||
| Related: | 3d32 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Complex structure of GABA type A receptor associated protein and its binding epitope on calreticulin
The 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile adaptor protein that plays an important role in intracellular vesicle trafficking, particularly in neuronal cells. We have investigated the structural determinants underlying the interaction of GABARAP with calreticulin using spectroscopic and crystallographic techniques. Specifically, we present the crystal structure of GABARAP in complex with its major binding epitope on the chaperone. Molecular modeling of a complex containing full-length calreticulin suggests a novel mode of substrate interaction, which may have functional implications for the calreticulin/calnexin family in general.
Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones., Thielmann Y, Weiergraber OH, Mohrluder J, Willbold D, FEBS J. 2009 Feb;276(4):1140-52. Epub 2009 Jan 16. PMID:19154346
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3DOW is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA. Relevant biological numbers for this protein at B10NUMB3R5
Reference
- Thielmann Y, Weiergraber OH, Mohrluder J, Willbold D. Structural framework of the GABARAP-calreticulin interface--implications for substrate binding to endoplasmic reticulum chaperones. FEBS J. 2009 Feb;276(4):1140-52. Epub 2009 Jan 16. PMID:19154346 doi:10.1111/j.1742-4658.2008.06857.x
Page seeded by OCA on Mon May 25 08:17:12 2009
Categories: Homo sapiens | Thielmann, Y. | Weiergraeber, O H. | Willbold, D. | Alpha-beta | Beta-grasp fold | Calcium | Chaperone | Cytoplasm | Cytoskeleton | Endoplasmic reticulum | Extracellular matrix | Golgi apparatus | Lectin | Membrane | Metal-binding | Microtubule | Protein transport | Secreted | Transport | Zinc
