This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3jv5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3jv5" [edit=sysop:move=sysop])
Line 1: Line 1:
-
{{STRUCTURE_3jv5| PDB=3jv5 | SCENE= }}
+
==Crystal structure of the dimerization domains p52 homodimer==
-
===Crystal structure of the dimerization domains p52 homodimer===
+
<StructureSection load='3jv5' size='340' side='right' caption='[[3jv5]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==Function==
+
<table><tr><td colspan='2'>[[3jv5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JV5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JV5 FirstGlance]. <br>
-
[[http://www.uniprot.org/uniprot/NFKB2_MOUSE NFKB2_MOUSE]] NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65 (By similarity).
+
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jtc|3jtc]], [[3juz|3juz]], [[3jv0|3jv0]], [[3jv4|3jv4]], [[3jv6|3jv6]]</td></tr>
-
 
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p52 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])</td></tr>
-
==About this Structure==
+
<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=3jv5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jv5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jv5 RCSB], [http://www.ebi.ac.uk/pdbsum/3jv5 PDBsum]</span></td></tr>
-
[[3jv5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JV5 OCA].
+
</table>
 +
__TOC__
 +
</StructureSection>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
-
[[Category: Ghosh, G.]]
+
[[Category: Ghosh, G]]
-
[[Category: Huang, D B.]]
+
[[Category: Huang, D B]]
-
[[Category: Vu, D.]]
+
[[Category: Vu, D]]
[[Category: Activator]]
[[Category: Activator]]
[[Category: Ank repeat]]
[[Category: Ank repeat]]

Revision as of 17:36, 18 December 2014

Crystal structure of the dimerization domains p52 homodimer

3jv5, resolution 2.65Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3jv5"
Personal tools