4B2B: Structure Of The Factor Xa-like Trypsin Variant Triple-ala (tgpa) In Complex With Eglin C

Citation:
Abstract
Abstract The energetics of macromolecular interactions are complex, particularly where protein flexibility is involved. Exploiting serendipitous differences in the plasticity of a series of closely related trypsin variants, we analyzed the enthalpic and entropic contributions accompanying interaction with L45K-eglin C. Binding of the four variants show significant differences in released heat, although the affinities vary little, in accordance with the principle of enthalpy-entropy compensation. Binding of the most disordered variant is almost entirely enthalpically driven, with practically no entropy change. As structures of the complexes reveal negligible differences in protein-inhibitor contacts, we conclude that solvent effects contribute significantly to binding affinities.
PDB ID: 4B2BDownload
MMDB ID: 101649
PDB Deposition Date: 2012/7/13
Updated in MMDB: 2012/08
Experimental Method:
x-ray diffraction
Resolution: 1.36  Å
Source Organism:
Bos taurus
Similar Structures:
Biological Unit for 4B2B: dimeric; determined by author and by software (PISA)
Molecular Components in 4B2B
Label Count Molecule
Proteins (2 molecules)
1
Cationic Trypsin(Gene symbol: PRSS1)
Molecule annotation
1
Eglin C
Molecule annotation
Chemicals (7 molecules)
1
1
2
3
3
2
4
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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