1CIQ

COMPLEX OF TWO FRAGMENTS OF CI2, RESIDUES 1-40 AND 41-64

Summary for 1CIQ

• Entry DOI: 10.2210/pdb1ciq/pdb
• Descriptor: CHYMOTRYPSIN INHIBITOR 2 (3 entities in total)
• Functional Keywords: cleaved inhibitor, serine protease inhibitor
• Biological source: Hordeum vulgare; More
• Total number of polymer chains: 2
• Total formula weight: 7331.64

Authors

Buckle, A.M.,Fersht, A.R. (deposition date: 1995-10-02, release date: 1996-03-08, Last modification date: 2024-02-07)

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

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: 9079381
DOI: 10.1016/S1359-0278(96)00031-4

Experimental method

X-RAY DIFFRACTION (2.2 Å)