2llx
From Proteopedia
(Difference between revisions)
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<StructureSection load='2llx' size='340' side='right' caption='[[2llx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2llx' size='340' side='right' caption='[[2llx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2llx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LLX OCA]. <br> | + | <table><tr><td colspan='2'>[[2llx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LLX OCA]. <br> |
| - | <b>[[Related_structure|Related:]]</b> [[1dt9|1dt9]], [[3e1y|3e1y]], [[2hst|2hst]], [[2ktv|2ktv]], [[2ktu|2ktu]]< | + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dt9|1dt9]], [[3e1y|3e1y]], [[2hst|2hst]], [[2ktv|2ktv]], [[2ktu|2ktu]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETF1, ERF1, RF1, SUP45L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2llx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2llx RCSB], [http://www.ebi.ac.uk/pdbsum/2llx PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></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=2llx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2llx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2llx RCSB], [http://www.ebi.ac.uk/pdbsum/2llx PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
The high-resolution NMR structure of the N-domain of human eRF1, responsible for stop codon recognition, has been determined in solution. The overall fold of the protein is the same as that found in the crystal structure. However, the structures of several loops, including those participating in stop codon decoding, are different. Analysis of the NMR relaxation data reveals that most of the regions with the highest structural discrepancy between the solution and solid states undergo internal motions on the ps-ns and ms time scales. The NMR data show that the N-domain of human eRF1 exists in two conformational states. The distribution of the residues having the largest chemical shift differences between the two forms indicates that helices alpha2 and alpha3, with the NIKS loop between them, can switch their orientation relative to the beta-core of the protein. Such structural plasticity may be essential for stop codon recognition by human eRF1. | The high-resolution NMR structure of the N-domain of human eRF1, responsible for stop codon recognition, has been determined in solution. The overall fold of the protein is the same as that found in the crystal structure. However, the structures of several loops, including those participating in stop codon decoding, are different. Analysis of the NMR relaxation data reveals that most of the regions with the highest structural discrepancy between the solution and solid states undergo internal motions on the ps-ns and ms time scales. The NMR data show that the N-domain of human eRF1 exists in two conformational states. The distribution of the residues having the largest chemical shift differences between the two forms indicates that helices alpha2 and alpha3, with the NIKS loop between them, can switch their orientation relative to the beta-core of the protein. Such structural plasticity may be essential for stop codon recognition by human eRF1. | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:53, 1 May 2014
Solution structure of the N-terminal domain of human polypeptide chain release factor eRF1
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