1KFZ

Solution Structure of C-terminal Sem-5 SH3 Domain (Ensemble of 16 Structures)

Summary for 1KFZ

• Entry DOI: 10.2210/pdb1kfz/pdb
• Related: 1K76
• NMR Information: BMRB: 5729
• Descriptor: SEX MUSCLE ABNORMAL PROTEIN 5 (1 entity in total)
• Functional Keywords: all beta protein, signaling protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 1
• Total formula weight: 7237.97

Authors

Ferreon, J.C.,Volk, D.E.,Luxon, B.A.,Gorenstein, D.,Hilser, V.J. (deposition date: 2001-11-24, release date: 2003-05-20, Last modification date: 2024-05-22)

Primary citation

Ferreon, J.C.,Volk, D.E.,Luxon, B.A.,Gorenstein, D.,Hilser, V.J.
Solution Structure, Dynamics and Thermodynamics of the Native State Ensemble of Sem-5 C-Terminal SH3 Domain
Biochemistry, 42:5582-5591, 2003

PubMed Abstract: Although the high-resolution structure of a protein may provide significant insight into which regions are important for function, it is well-known that proteins undergo significant conformational fluctuations, even under native conditions. This suggests that the static structure alone may not provide sufficient information for elucidation of the thermodynamic determinants of biological function and that an accurate molecular-level description of function requires knowledge of the nature and energetics of the conformational states that constitute the native state ensemble. Here the native state ensemble of the C-terminal src homology domain-3 (C-SH3) from Caenorhabditis elegans Sem-5 has been studied using a variety of high-resolution biophysical techniques. In addition to determining the first solution structure of the unliganded protein, we have performed (15)N relaxation and native state hydrogen-deuterium exchange. It is observed that the regions of greatest structural variabilility also show low protection and order parameters, suggesting a higher degree of conformational diversity. These flexible regions also coincide with those regions of Sem-5 that have been predicted by the COREX algorithm to be unfolded in many of the most probable conformational states within the native state ensemble. The implications of this agreement and the potential role of conformational heterogeneity of the observed biophysical properties are discussed.

PubMed: 12741814
DOI: 10.1021/bi030005j

Experimental method

SOLUTION NMR