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{{Theoretical_model}} | |||
==HOMOLOGY MODELING OF THE ABL-SH3 DOMAIN== | |||
<StructureSection load='1abl' size='340' side='right'caption='[[1abl]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ABL FirstGlance]. <br> | |||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1abl FirstGlance], [https://www.ebi.ac.uk/pdbsum/1abl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1abl ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A tertiary structure model of the Abl-SH3 domain is predicted by using homology modeling techniques coupled to molecular dynamics simulations. Two template proteins were used, Fyn-SH3 and Spc-SH3. The refined model was extensively checked for errors using criteria based on stereochemistry, packing, solvation free-energy, accessible surface areas, and contact analyses. The different checking methods do not totally agree, as each one evaluates a different characteristic of protein structures. Several zones of the protein are more susceptible to incorporating errors. These include residues 13, 15, 35, 39, 45, 46, 50, and 60. An interesting finding is that the measurement of the C alpha chirality correlated well with the rest of the criteria, suggesting that this parameter might be a good indicator of correct local conformation. Deviations of more than 4 degrees may be indicative of poor local structure. | |||
Homology modeling of the Abl-SH3 domain.,Pisabarro MT, Ortiz AR, Serrano L, Wade RC Proteins. 1994 Nov;20(3):203-15. PMID:7892170<ref>PMID:7892170</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1abl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Theoretical Model]] | |||
[[Category: Large Structures]] | |||
[[Category: Ortiz, A R]] | |||
[[Category: Pisabarro, M T]] | |||
[[Category: Serrano, L]] | |||
[[Category: Wade, R C]] | |||
Latest revision as of 12:44, 26 May 2021
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HOMOLOGY MODELING OF THE ABL-SH3 DOMAINHOMOLOGY MODELING OF THE ABL-SH3 DOMAIN
Structural highlights
Publication Abstract from PubMedA tertiary structure model of the Abl-SH3 domain is predicted by using homology modeling techniques coupled to molecular dynamics simulations. Two template proteins were used, Fyn-SH3 and Spc-SH3. The refined model was extensively checked for errors using criteria based on stereochemistry, packing, solvation free-energy, accessible surface areas, and contact analyses. The different checking methods do not totally agree, as each one evaluates a different characteristic of protein structures. Several zones of the protein are more susceptible to incorporating errors. These include residues 13, 15, 35, 39, 45, 46, 50, and 60. An interesting finding is that the measurement of the C alpha chirality correlated well with the rest of the criteria, suggesting that this parameter might be a good indicator of correct local conformation. Deviations of more than 4 degrees may be indicative of poor local structure. Homology modeling of the Abl-SH3 domain.,Pisabarro MT, Ortiz AR, Serrano L, Wade RC Proteins. 1994 Nov;20(3):203-15. PMID:7892170[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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