NEW PROTEIN FOLD REVEALED BY A 2.3 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF NERVE GROWTH FACTOR
There is a Quite Interesting Protein Structure article for this entry.
The structure was published by McDonald, N.Q., Lapatto, R., Murray-Rust, J., Gunning, J., Wlodawer, A., and Blundell, T.L., in 1991 in a paper entitled "New protein fold revealed by a 2.3-A resolution crystal structure of nerve growth factor." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1993.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of BETA-NERVE GROWTH FACTOR. This molecule has the UniProt identifier P01139 (NGF_MOUSE). The sample contained 107 residues which is < 90% of the natural sequence. Out of 107 residues 107 were observed and are deposited in the PDB.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: