2ldc: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ldc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDC FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ldc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LDC FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MK8:2-METHYL-L-NORLEUCINE'>MK8</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ldc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldc OCA], [https://pdbe.org/2ldc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldc RCSB], [https://www.ebi.ac.uk/pdbsum/2ldc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldc ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ldc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ldc OCA], [https://pdbe.org/2ldc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ldc RCSB], [https://www.ebi.ac.uk/pdbsum/2ldc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ldc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 04:09, 21 November 2024
Solution structure of the estrogen receptor-binding stapled peptide SP1 (Ac-HXILHXLLQDS-NH2)Solution structure of the estrogen receptor-binding stapled peptide SP1 (Ac-HXILHXLLQDS-NH2)
Structural highlights
DiseaseNCOA2_HUMAN Note=Chromosomal aberrations involving NCOA2 may be a cause of acute myeloid leukemias. Inversion inv(8)(p11;q13) generates the KAT6A-NCOA2 oncogene, which consists of the N-terminal part of KAT6A and the C-terminal part of NCOA2/TIF2. KAT6A-NCOA2 binds to CREBBP and disrupts its function in transcription activation. FunctionNCOA2_HUMAN Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues.[1] Publication Abstract from PubMedSynthetic peptides that specifically bind nuclear hormone receptors offer an alternative approach to small molecules for the modulation of receptor signaling and subsequent gene expression. Here we describe the design of a series of novel stapled peptides that bind the coactivator peptide site of estrogen receptors. Using a number of biophysical techniques, including crystal structure analysis of receptor-stapled peptide complexes, we describe in detail the molecular interactions and demonstrate that all-hydrocarbon staples modulate molecular recognition events. The findings have implications for the design of stapled peptides in general. Design and structure of stapled peptides binding to estrogen receptors.,Phillips C, Roberts LR, Schade M, Bazin R, Bent A, Davies NL, Moore R, Pannifer AD, Pickford AR, Prior SH, Read CM, Scott A, Brown DG, Xu B, Irving SL J Am Chem Soc. 2011 Jun 29;133(25):9696-9. Epub 2011 Jun 6. PMID:21612236[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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