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| {{STRUCTURE_1gnu| PDB=1gnu | SCENE= }} | | {{STRUCTURE_1gnu| PDB=1gnu | SCENE= }} |
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| '''GABA(A) RECEPTOR ASSOCIATED PROTEIN GABARAP'''
| | ===GABA(A) RECEPTOR ASSOCIATED PROTEIN GABARAP=== |
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| ==Overview==
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| The gamma-aminobutyric acid receptor type A (GABA(A)) receptor-associated protein (GABARAP) has been reported to mediate the interaction between the GABA(A) receptor and microtubules. We present the three-dimensional structure of GABARAP obtained by x-ray diffraction at 1.75 A resolution. The structure was determined by molecular replacement using the structure of the homologous protein GATE-16. NMR spectroscopy of isotope-labeled GABARAP showed the structure in solution to be compatible with the overall fold but showed evidence of conformation heterogeneity that is not apparent in the crystal structure. We assessed the binding of GABARAP to peptides derived from reported binding partner proteins, including the M3-M4 loop of the gamma2 subunit of the GABA(A) receptor and the acidic carboxyl-terminal tails of human alpha- and beta-tubulin. There is a small area of concentrated positive charge on one surface of GABARAP, which we found interacts weakly with all peptides tested, but we found no evidence for specific binding to the proposed physiological target peptides. These results are compatible with a more general role in membrane targeting and transportation for the GABARAP family of proteins. | | The line below this paragraph, {{ABSTRACT_PUBMED_11729197}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11729197 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11729197}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Transport]] | | [[Category: Transport]] |
| [[Category: Ubiquitin-like]] | | [[Category: Ubiquitin-like]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:48:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:34:38 2008'' |
