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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)search. 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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A BETA-NERVE GROWTH FACTOR P01139 (131-237) (NGF_MOUSE)search Mus musculussearch 100% 107 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P01139 (131 - 237) BETA-NERVE GROWTH FACTOR Mus musculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P01139) Neurotrophinsearch Cystine-knot cytokinessearch PF00243: Nerve growth factor familysearch

Chain ID Molecular function (GO)
A (P01139) receptor bindingsearch

Chain InterPro annotation
A Nerve growth factor-relatedsearch Nerve growth factor conserved sitesearch Nerve growth factor-likesearch Nerve growth factor, beta subunitsearch