1B7M

VERIFICATION OF SPMP USING MUTANT HUMAN LYSOZYMES

1B7M の概要

• エントリーDOI: 10.2210/pdb1b7m/pdb
• 分子名称: PROTEIN (LYSOZYME), SODIUM ION (3 entities in total)
• 機能のキーワード: mutant stability, human lysozyme, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P61626
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14803.80

構造登録者

Takano, K.,Ota, M.,Ogasahara, K.,Yamagata, Y.,Nishikawa, K.,Yutani, K. (登録日: 1999-01-24, 公開日: 1999-01-27, 最終更新日: 2024-11-13)

主引用文献

Takano, K.,Ota, M.,Ogasahara, K.,Yamagata, Y.,Nishikawa, K.,Yutani, K.
Experimental verification of the 'stability profile of mutant protein' (SPMP) data using mutant human lysozymes.
Protein Eng., 12:663-672, 1999

PubMed Abstract: The stability profile of mutant protein (SPMP) (Ota,M., Kanaya,S. and Nishikawa,K., 1995, J. Mol. Biol., 248, 733-738) estimates the changes in conformational stability due to single amino acid substitutions using a pseudo-energy potential developed for evaluating structure-sequence compatibility in the structure prediction method, the 3D-1D compatibility evaluation. Nine mutant human lysozymes expected to significantly increase in stability from SPMP were constructed, in order to experimentally verify the reliability of SPMP. The thermodynamic parameters for denaturation and crystal structures of these mutant proteins were determined. One mutant protein was stabilized as expected, compared with the wild-type protein. However, the others were not stabilized even though the structural changes were subtle, indicating that SPMP overestimates the increase in stability or underestimates negative effects due to substitution. The stability changes in the other mutant human lysozymes previously reported were also analyzed by SPMP. The correlation of the stability changes between the experiment and prediction depended on the types of substitution: there were some correlations for proline mutants and cavity-creating mutants, but no correlation for mutants related to side-chain hydrogen bonds. The present results may indicate some additional factors that should be considered in the calculation of SPMP, suggesting that SPMP can be refined further.

PubMed: 10469827
DOI: 10.1093/protein/12.8.663

実験手法

X-RAY DIFFRACTION (2.2 Å)