1gnu: Difference between revisions
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==Overview== | ==Overview== | ||
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 ... | 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. | ||
==About this Structure== | ==About this Structure== | ||
1GNU is a | 1GNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NI as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: NI. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GNU OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: ubiquitin-like]] | [[Category: ubiquitin-like]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:41:01 2007'' | ||
Revision as of 15:35, 5 November 2007
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GABA(A) RECEPTOR ASSOCIATED PROTEIN GABARAP
OverviewOverview
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.
About this StructureAbout this Structure
1GNU is a Single protein structure of sequence from Homo sapiens with NI as ligand. Structure known Active Site: NI. Full crystallographic information is available from OCA.
ReferenceReference
The X-ray crystal structure and putative ligand-derived peptide binding properties of gamma-aminobutyric acid receptor type A receptor-associated protein., Knight D, Harris R, McAlister MS, Phelan JP, Geddes S, Moss SJ, Driscoll PC, Keep NH, J Biol Chem. 2002 Feb 15;277(7):5556-61. Epub 2001 Nov 29. PMID:11729197
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