1am9
From Proteopedia
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|PDB= 1am9 |SIZE=350|CAPTION= <scene name='initialview01'>1am9</scene>, resolution 2.300Å | |PDB= 1am9 |SIZE=350|CAPTION= <scene name='initialview01'>1am9</scene>, resolution 2.300Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1am9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1am9 OCA], [http://www.ebi.ac.uk/pdbsum/1am9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1am9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Burley, S K.]] | [[Category: Burley, S K.]] | ||
[[Category: Parraga, A.]] | [[Category: Parraga, A.]] | ||
| - | [[Category: MG]] | ||
[[Category: basic-helix-loop-helix-leucine zipper]] | [[Category: basic-helix-loop-helix-leucine zipper]] | ||
[[Category: complex (transcription regulation/dna)]] | [[Category: complex (transcription regulation/dna)]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:10 2008'' |
Revision as of 15:43, 30 March 2008
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| , resolution 2.300Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN SREBP-1A BOUND TO LDL RECEPTOR PROMOTER
Overview
BACKGROUND: The sterol regulatory element binding proteins (SREBPs) are helix-loop-helix transcriptional activators that control expression of genes encoding proteins essential for cholesterol biosynthesis/uptake and fatty acid biosynthesis. Unlike helix-loop-helix proteins that recognize symmetric E-boxes (5'-CANNTG-3'), the SREBPs have a tyrosine instead of a conserved arginine in their basic regions. This difference allows recognition of an asymmetric sterol regulatory element (StRE, 5'-ATCACCCAC-3'). RESULTS: The 2.3 A resolution co-crystal structure of the DNA-binding portion of SREBP-1a bound to an StRE reveals a quasi-symmetric homodimer with an asymmetric DNA-protein interface. One monomer binds the E-box half site of the StRE (5'-ATCAC-3') using sidechain-base contacts typical of other helix-loop-helix proteins. The non-E-box half site (5'-GTGGG-3') is recognized through entirely different protein-DNA contacts. CONCLUSIONS: Although the SREBPs are structurally similar to the E-box-binding helix-loop-helix proteins, the Arg-->Tyr substitution yields dramatically different DNA-binding properties that explain how they recognize StREs and regulate expression of genes important for membrane biosynthesis.
About this Structure
1AM9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Co-crystal structure of sterol regulatory element binding protein 1a at 2.3 A resolution., Parraga A, Bellsolell L, Ferre-D'Amare AR, Burley SK, Structure. 1998 May 15;6(5):661-72. PMID:9634703
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