3i8c
From Proteopedia
(Difference between revisions)
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==Crystal Structure of DDB1 in Complex with the H-Box Motif of WDR21A== | ==Crystal Structure of DDB1 in Complex with the H-Box Motif of WDR21A== | ||
| - | <StructureSection load='3i8c' size='340' side='right' caption='[[3i8c]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='3i8c' size='340' side='right'caption='[[3i8c]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3i8c]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3i8c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I8C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I8C FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b5m|2b5m]], [[3i7h|3i7h]], [[3i7k|3i7k]], [[3i7l|3i7l]], [[3i7n|3i7n]], [[3i7o|3i7o]], [[3i7p|3i7p]], [[3i89|3i89]], [[3i8e|3i8e]]</td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b5m|2b5m]], [[3i7h|3i7h]], [[3i7k|3i7k]], [[3i7l|3i7l]], [[3i7n|3i7n]], [[3i7o|3i7o]], [[3i7p|3i7p]], [[3i89|3i89]], [[3i8e|3i8e]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB1, XAP1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB1, XAP1 ([https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8c OCA], [https://pdbe.org/3i8c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i8c RCSB], [https://www.ebi.ac.uk/pdbsum/3i8c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i8c ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DDB1_HUMAN DDB1_HUMAN]] Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2.<ref>PMID:12732143</ref> <ref>PMID:15448697</ref> <ref>PMID:14739464</ref> <ref>PMID:15882621</ref> <ref>PMID:16260596</ref> <ref>PMID:16482215</ref> <ref>PMID:17079684</ref> <ref>PMID:16407242</ref> <ref>PMID:16407252</ref> <ref>PMID:16678110</ref> <ref>PMID:16940174</ref> <ref>PMID:17041588</ref> <ref>PMID:16473935</ref> <ref>PMID:18593899</ref> <ref>PMID:18381890</ref> <ref>PMID:18332868</ref> [[https://www.uniprot.org/uniprot/DCAF4_HUMAN DCAF4_HUMAN]] May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.<ref>PMID:16949367</ref> <ref>PMID:16964240</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Breugel, P C.V]] | [[Category: Breugel, P C.V]] | ||
[[Category: Li, T]] | [[Category: Li, T]] | ||
Revision as of 11:00, 13 April 2022
Crystal Structure of DDB1 in Complex with the H-Box Motif of WDR21A
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Categories: Human | Large Structures | Breugel, P C.V | Li, T | Robert, E I | Strubin, M | Zheng, N | Alternative splicing | Cytoplasm | Dcaf4 | Ddb1 | Dna damage | Dna repair | Dna-binding | H-box motif | Host-virus interaction | Nucleus | Phosphoprotein | Polymorphism | Protein binding | Ubl conjugation | Ubl conjugation pathway | Wd repeat | Wdr21a
