1ICL
SOLUTION STRUCTURE OF DESIGNED BETA-SHEET MINI-PROTEIN TH1OX
Summary for 1ICL
| Entry DOI | 10.2210/pdb1icl/pdb |
| Related | 1IC9 1ICO |
| Descriptor | TH1OX (1 entity in total) |
| Functional Keywords | de novo protein design three-stranded beta-sheet mini-protein motif th motif, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 3254.73 |
| Authors | Ottesen, J.J.,Imperiali, B. (deposition date: 2001-04-02, release date: 2001-04-11, Last modification date: 2024-10-16) |
| Primary citation | Ottesen, J.J.,Imperiali, B. Design of a discretely folded mini-protein motif with predominantly beta-structure. Nat.Struct.Biol., 8:535-539, 2001 Cited by PubMed Abstract: Here we report the creation of a predominantly beta-structured mini-protein motif. The design target is based on the naturally occurring toxin hand (TH) motifs that are composed of four disulfide bonds and three loops that form a 'hand'. Analysis and subsequent modification of several generations of mini-proteins produced the final 29-residue mini-protein. The structured motif of this new mini-protein provides insight into the compensatory changes that result in the formation of a tightly packed hydrophobic core in a small, globular beta-structure motif. Additionally, this mini-motif represents a new, distinct surface topology for protein design and a valuable, yet compact, model system for the study of beta-sheet structure in water. PubMed: 11373623DOI: 10.1038/88604 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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