4le9: Difference between revisions
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''' | ==Crystal structure of a chimeric c-Src-SH3 domain== | ||
<StructureSection load='4le9' size='340' side='right' caption='[[4le9]], [[Resolution|resolution]] 1.34Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4le9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LE9 OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fj5|3fj5]], [[4jz4|4jz4]], [[4jz3|4jz3]]</td></tr> | |||
<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=4le9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4le9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4le9 RCSB], [http://www.ebi.ac.uk/pdbsum/4le9 PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. We have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain. Crystals of the chimeric protein show a single molecule in the asymmetric unit, which appears in an unfolded-like structure that upon generation of the symmetry related molecules reveals the presence of a domain swapped dimer where both, RT- and n-Src loops, act as hinge loops. In contrast, the fold of the diverging type II beta-turn and the distal loop are well conserved. Our results are the first evidence for the presence of a structured diverging type II beta-turn in an unfolded-like intermediate of the c-Src-SH3 domain, which can be stabilized by interactions from the beta-strands of the same polypeptide chain or from a neighboring one. Futhermore, this crystallographic structure opens a unique opportunity to study the effect of the amino acid sequence of the hinge loops on the 3D domain swapping process of c-Src-SH3. | |||
3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops.,Camara-Artigas A, Martinez-Rodriguez S, Ortiz-Salmeron E, Martin-Garcia JM J Struct Biol. 2014 Apr;186(1):195-203. doi: 10.1016/j.jsb.2014.02.007. Epub 2014, Feb 17. PMID:24556574<ref>PMID:24556574</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Non-specific protein-tyrosine kinase]] | |||
[[Category: Camara-Artigas, A.]] | |||
[[Category: Martin-Garcia, J M.]] | |||
[[Category: Martinez-Rodriguez, S.]] | |||
[[Category: Ortiz-Salmeron, E.]] | |||
[[Category: Beta shandwich]] | |||
[[Category: Kinase]] | |||
[[Category: Phosphorylation]] | |||
[[Category: Proly proline rich motif]] | |||
[[Category: Sh3]] | |||
[[Category: Transferase]] | |||
Revision as of 11:12, 7 May 2014
Crystal structure of a chimeric c-Src-SH3 domainCrystal structure of a chimeric c-Src-SH3 domain
Structural highlights
Publication Abstract from PubMedIn the Src Homology 3 domain (SH3) the RT and n-Src loops form a pocket that accounts for the specificity and affinity in binding of proline rich motifs (PRMs), while the distal and diverging turns play a key role in the folding of the protein. We have solved the structure of a chimeric mutant c-Src-SH3 domain where specific residues at the RT- and n-Src-loops have been replaced by those present in the corresponding Abl-SH3 domain. Crystals of the chimeric protein show a single molecule in the asymmetric unit, which appears in an unfolded-like structure that upon generation of the symmetry related molecules reveals the presence of a domain swapped dimer where both, RT- and n-Src loops, act as hinge loops. In contrast, the fold of the diverging type II beta-turn and the distal loop are well conserved. Our results are the first evidence for the presence of a structured diverging type II beta-turn in an unfolded-like intermediate of the c-Src-SH3 domain, which can be stabilized by interactions from the beta-strands of the same polypeptide chain or from a neighboring one. Futhermore, this crystallographic structure opens a unique opportunity to study the effect of the amino acid sequence of the hinge loops on the 3D domain swapping process of c-Src-SH3. 3D domain swapping in a chimeric c-Src SH3 domain takes place through two hinge loops.,Camara-Artigas A, Martinez-Rodriguez S, Ortiz-Salmeron E, Martin-Garcia JM J Struct Biol. 2014 Apr;186(1):195-203. doi: 10.1016/j.jsb.2014.02.007. Epub 2014, Feb 17. PMID:24556574[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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