1qrv
From Proteopedia
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|PDB= 1qrv |SIZE=350|CAPTION= <scene name='initialview01'>1qrv</scene>, resolution 2.20Å | |PDB= 1qrv |SIZE=350|CAPTION= <scene name='initialview01'>1qrv</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</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=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2lef|2LEF]], [[1hrz|1HRZ]], [[1hma|1HMA]], [[1hmf|1HMF]], [[1cg7|1CG7]], [[1ckt|1CKT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qrv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qrv OCA], [http://www.ebi.ac.uk/pdbsum/1qrv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qrv RCSB]</span> | ||
}} | }} | ||
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[[Category: IV, F V.Murphy.]] | [[Category: IV, F V.Murphy.]] | ||
[[Category: Sweet, R M.]] | [[Category: Sweet, R M.]] | ||
| - | [[Category: NA]] | ||
[[Category: hmg domain]] | [[Category: hmg domain]] | ||
[[Category: non-sequence specific chromosomal protein hmg-d]] | [[Category: non-sequence specific chromosomal protein hmg-d]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''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 23:18:07 2008'' |
Revision as of 20:18, 30 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , | ||||||
| Related: | 2LEF, 1HRZ, 1HMA, 1HMF, 1CG7, 1CKT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE COMPLEX OF HMG-D AND DNA
Overview
The high mobility group (HMG) chromosomal proteins, which are common to all eukaryotes, bind DNA in a non-sequence-specific fashion to promote chromatin function and gene regulation. They interact directly with nucleosomes and are believed to be modulators of chromatin structure. They are also important in V(D)J recombination and in activating a number of regulators of gene expression, including p53, Hox transcription factors and steroid hormone receptors, by increasing their affinity for DNA. The X-ray crystal structure, at 2.2 A resolution, of the HMG domain of the Drosophila melanogaster protein, HMG-D, bound to DNA provides the first detailed view of a chromosomal HMG domain interacting with linear DNA and reveals the molecular basis of non-sequence-specific DNA recognition. Ser10 forms water-mediated hydrogen bonds to DNA bases, and Val32 with Thr33 partially intercalates the DNA. These two 'sequence-neutral' mechanisms of DNA binding substitute for base-specific hydrogen bonds made by equivalent residues of the sequence-specific HMG domain protein, lymphoid enhancer factor-1. The use of multiple intercalations and water-mediated DNA contacts may prove to be generally important mechanisms by which chromosomal proteins bind to DNA in the minor groove.
About this Structure
1QRV is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition., Murphy FV 4th, Sweet RM, Churchill ME, EMBO J. 1999 Dec 1;18(23):6610-8. PMID:10581235
Page seeded by OCA on Sun Mar 30 23:18:07 2008
