3mcb: Difference between revisions
Jump to navigation
Jump to search
m Protected "3mcb" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image: | ==Crystal structure of NAC domains of human nascent polypeptide-associated complex (NAC)== | ||
<StructureSection load='3mcb' size='340' side='right' caption='[[3mcb]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3mcb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MCB FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mce|3mce]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Alpha NAC, HSD48, NACA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Beta NAC (BTF3b), BTF3, NACB, OK/SW-cl.8 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mcb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mcb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mcb RCSB], [http://www.ebi.ac.uk/pdbsum/3mcb PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mc/3mcb_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nascent polypeptide associated complex (NAC) and its two isolated subunits, alphaNAC and betaNAC, play important roles in nascent peptide targeting. We determined a 1.9 A resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 A resolution crystal structure of alphaNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and alphaNAC homodimerization. We found that the NAC domains of alphaNAC and betaNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a betaNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC. | |||
Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit.,Wang L, Zhang W, Wang L, Zhang XC, Li X, Rao Z Protein Cell. 2010 Apr;1(4):406-16. Epub 2010 May 8. PMID:21203952<ref>PMID:21203952</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Li, X M.]] | [[Category: Li, X M.]] | ||
Revision as of 13:26, 28 May 2014
Crystal structure of NAC domains of human nascent polypeptide-associated complex (NAC)Crystal structure of NAC domains of human nascent polypeptide-associated complex (NAC)
Structural highlights
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 PubMedNascent polypeptide associated complex (NAC) and its two isolated subunits, alphaNAC and betaNAC, play important roles in nascent peptide targeting. We determined a 1.9 A resolution crystal structure of the interaction core of NAC heterodimer and a 2.4 A resolution crystal structure of alphaNAC NAC domain homodimer. These structures provide detailed information of NAC heterodimerization and alphaNAC homodimerization. We found that the NAC domains of alphaNAC and betaNAC share very similar folding despite of their relative low identity of amino acid sequences. Furthermore, different electric charge distributions of the two subunits at the NAC interface provide an explanation to the observation that the heterodimer of NAC complex is more stable than the single subunit homodimer. In addition, we successfully built a betaNAC NAC domain homodimer model based on homologous modeling, suggesting that NAC domain dimerization is a general property of the NAC family. These 3D structures allow further studies on structure-function relationship of NAC. Crystal structures of NAC domains of human nascent polypeptide-associated complex (NAC) and its alphaNAC subunit.,Wang L, Zhang W, Wang L, Zhang XC, Li X, Rao Z Protein Cell. 2010 Apr;1(4):406-16. Epub 2010 May 8. PMID:21203952[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||