1CIR
COMPLEX OF TWO FRAGMENTS OF CI2 [(1-40)(DOT)(41-64)]
Summary for 1CIR
| Entry DOI | 10.2210/pdb1cir/pdb |
| Descriptor | CHYMOTRYPSIN INHIBITOR 2 (2 entities in total) |
| Functional Keywords | serine protease inhibitor |
| Biological source | Hordeum vulgare More |
| Total number of polymer chains | 2 |
| Total formula weight | 7301.55 |
| Authors | Davis, B.J.,Fersht, A.R. (deposition date: 1995-10-02, release date: 1996-01-29, Last modification date: 2024-05-22) |
| Primary citation | Neira, J.L.,Davis, B.,Ladurner, A.G.,Buckle, A.M.,Gay Gde, P.,Fersht, A.R. Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism Structure Fold.Des., 1:189-208, 1996 Cited by PubMed Abstract: Single-module proteins, such as chymotrypsin inhibitor 2 (CI2), fold as a single cooperative unit. To solve its folding pathway, we must characterize, under conditions that favour folding, its denatured state, its transition state, and its final folded structure. To obtain a "denatured state' that can readily be thus characterized, we have used a trick of cleaving CI2 into two complementary fragments that associate and fold in a similar way to intact protein. PubMed: 9079381DOI: 10.1016/S1359-0278(96)00031-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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