First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.
3gg3
From Proteopedia
| 3gg3, resolution 2.25Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | |||||||||
| Gene: | PCAF (Homo sapiens) | ||||||||
| Activity: | Histone acetyltransferase, with EC number 2.3.1.48 | ||||||||
| |||||||||
| |||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal Structure of the Bromodomain of Human PCAF
Bromodomains (BRDs) are protein interaction modules that specifically recognize epsilon-N-lysine acetylation motifs, a key event in the reading process of epigenetic marks. The 61 BRDs in the human genome cluster into eight families based on structure/sequence similarity. Here, we present 29 high-resolution crystal structures, covering all BRD families. Comprehensive crossfamily structural analysis identifies conserved and family-specific structural features that are necessary for specific acetylation-dependent substrate recognition. Screening of more than 30 representative BRDs against systematic histone-peptide arrays identifies new BRD substrates and reveals a strong influence of flanking posttranslational modifications, such as acetylation and phosphorylation, suggesting that BRDs recognize combinations of marks rather than singly acetylated sequences. We further uncovered a structural mechanism for the simultaneous binding and recognition of diverse diacetyl-containing peptides by BRD4. These data provide a foundation for structure-based drug design of specific inhibitors for this emerging target family.
Histone recognition and large-scale structural analysis of the human bromodomain family., Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S, Cell. 2012 Mar 30;149(1):214-31. PMID:22464331
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3gg3 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Filippakopoulos P, Picaud S, Mangos M, Keates T, Lambert JP, Barsyte-Lovejoy D, Felletar I, Volkmer R, Muller S, Pawson T, Gingras AC, Arrowsmith CH, Knapp S. Histone recognition and large-scale structural analysis of the human bromodomain family. Cell. 2012 Mar 30;149(1):214-31. PMID:22464331 doi:10.1016/j.cell.2012.02.013
Categories: Histone acetyltransferase | Homo sapiens | Arrowsmith, C H. | Bountra, C. | Delft, F Von. | Edwards, A M. | Fedorov, O. | Filippakopoulos, P. | Keates, T. | Knapp, S. | Picaud, S. | Rehana, K. | SGC, Structural Genomics Consortium. | Ugochukwu, E. | Weigelt, J. | Acyltransferase | Bromodomain | Cell cycle | Crebbp-associated factor | Gcn5 | Gcn5l | Host-virus interaction | Kat2b | Nucleus | P/caf | P300/cbp-associated factor | Pcaf | Phosphoprotein | Sgc | Structural genomics consortium | Transcription | Transcription regulation | Transferase
