1YMZ
CC45, An Artificial WW Domain Designed Using Statistical Coupling Analysis
Summary for 1YMZ
| Entry DOI | 10.2210/pdb1ymz/pdb |
| NMR Information | BMRB: 6530 |
| Descriptor | CC45 (1 entity in total) |
| Functional Keywords | artificial protein, computational design, unknown function |
| Total number of polymer chains | 1 |
| Total formula weight | 5054.72 |
| Authors | Socolich, M.,Lockless, S.W.,Russ, W.P.,Lee, H.,Gardner, K.H.,Ranganathan, R. (deposition date: 2005-01-22, release date: 2005-09-27, Last modification date: 2024-05-22) |
| Primary citation | Socolich, M.,Lockless, S.W.,Russ, W.P.,Lee, H.,Gardner, K.H.,Ranganathan, R. Evolutionary information for specifying a protein fold. Nature, 437:512-518, 2005 Cited by PubMed Abstract: Classical studies show that for many proteins, the information required for specifying the tertiary structure is contained in the amino acid sequence. Here, we attempt to define the sequence rules for specifying a protein fold by computationally creating artificial protein sequences using only statistical information encoded in a multiple sequence alignment and no tertiary structure information. Experimental testing of libraries of artificial WW domain sequences shows that a simple statistical energy function capturing coevolution between amino acid residues is necessary and sufficient to specify sequences that fold into native structures. The artificial proteins show thermodynamic stabilities similar to natural WW domains, and structure determination of one artificial protein shows excellent agreement with the WW fold at atomic resolution. The relative simplicity of the information used for creating sequences suggests a marked reduction to the potential complexity of the protein-folding problem. PubMed: 16177782DOI: 10.1038/nature03991 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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