1nkp

From Proteopedia

(Difference between revisions)

Revision as of 08:52, 2 December 2020

Crystal structure of Myc-Max recognizing DNA

Structural highlights

1nkp is a 8 chain structure with sequence from Human. The April 2009 RCSB PDB Molecule of the Month feature on Oct and Sox Transcription Factors by David Goodsell is 10.2210/rcsb_pdb/mom_2009_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Myc (HUMAN), Max (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[MYC_HUMAN] Note=Overexpression of MYC is implicated in the etiology of a variety of hematopoietic tumors. Note=A chromosomal aberration involving MYC may be a cause of a form of B-cell chronic lymphocytic leukemia. Translocation t(8;12)(q24;q22) with BTG1. Defects in MYC are a cause of Burkitt lymphoma (BL) [MIM:113970]. A form of undifferentiated malignant lymphoma commonly manifested as a large osteolytic lesion in the jaw or as an abdominal mass. Note=Chromosomal aberrations involving MYC are usually found in Burkitt lymphoma. Translocations t(8;14), t(8;22) or t(2;8) which juxtapose MYC to one of the heavy or light chain immunoglobulin gene loci.

Function

[MAX_HUMAN] Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MYC or MAD which recognizes the core sequence 5'-CAC[GA]TG-3'. The MYC-MAX complex is a transcriptional activator, whereas the MAD-MAX complex is a repressor. May repress transcription via the recruitment of a chromatin remodeling complex containing H3 'Lys-9' histone methyltransferase activity. [MYC_HUMAN] Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Seems to activate the transcription of growth-related genes.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

X-ray structures of the basic/helix-loop-helix/leucine zipper (bHLHZ) domains of Myc-Max and Mad-Max heterodimers bound to their common DNA target (Enhancer or E box hexanucleotide, 5'-CACGTG-3') have been determined at 1.9 A and 2.0 A resolution, respectively. E box recognition by these two structurally similar transcription factor pairs determines whether a cell will divide and proliferate (Myc-Max) or differentiate and become quiescent (Mad-Max). Deregulation of Myc has been implicated in the development of many human cancers, including Burkitt's lymphoma, neuroblastomas, and small cell lung cancers. Both quasisymmetric heterodimers resemble the symmetric Max homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these three evolutionarily related DNA-binding proteins. The Myc-Max heterodimer, but not its Mad-Max counterpart, dimerizes to form a bivalent heterotetramer, which explains how Myc can upregulate expression of genes with promoters bearing widely separated E boxes.

X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors.,Nair SK, Burley SK Cell. 2003 Jan 24;112(2):193-205. PMID:12553908^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nair SK, Burley SK. X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors. Cell. 2003 Jan 24;112(2):193-205. PMID:12553908

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nkp"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Myc-Max recognizing DNA==
-<StructureSection load='1nkp' size='340' side='right' caption='[[1nkp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1nkp' size='340' side='right'caption='[[1nkp]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1nkp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The April 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Oct and Sox Transcription Factors''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_4 10.2210/rcsb_pdb/mom_2009_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NKP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1nkp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. The April 2009 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Oct and Sox Transcription Factors''  by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2009_4 10.2210/rcsb_pdb/mom_2009_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NKP FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Myc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Max ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nkp OCA], [http://pdbe.org/1nkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nkp RCSB], [http://www.ebi.ac.uk/pdbsum/1nkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nkp ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nkp OCA], [http://pdbe.org/1nkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nkp RCSB], [http://www.ebi.ac.uk/pdbsum/1nkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nkp ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 32: / Line 32: @@
 ==See Also==
+*[[C-Myc|C-Myc]]
 *[[Teaching Scenes%2C Tutorials%2C and Educators' Pages|Teaching Scenes%2C Tutorials%2C and Educators' Pages]]
 == References ==
@@ Line 38: / Line 39: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Oct and Sox Transcription Factors]]
 [[Category: RCSB PDB Molecule of the Month]]

1nkp

From Proteopedia

Revision as of 08:52, 2 December 2020

Crystal structure of Myc-Max recognizing DNA

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox