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1abl
From Proteopedia
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| 1abl () | |
|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB |
| Coordinates: | save as pdb, mmCIF, xml |
HOMOLOGY MODELING OF THE ABL-SH3 DOMAIN
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
Full crystallographic information is available from OCA.
Reference
- Pisabarro MT, Ortiz AR, Serrano L, Wade RC. Homology modeling of the Abl-SH3 domain. Proteins. 1994 Nov;20(3):203-15. PMID:7892170 doi:10.1002/prot.340200302
Page seeded by OCA on Thu Apr 8 08:24:34 2010
