1M16

Human Acidic Fibroblast Growth Factor. 141 Amino Acid Form with Amino Terminal His Tag and Leu 44 Replaced with Phe (L44F), Leu 73 Replaced with Val (L73V), Val 109 Replaced with Leu (V109L) and Cys 117 Replaced with Val (C117V).

Summary for 1M16

• Entry DOI: 10.2210/pdb1m16/pdb
• Related: 1JQZ
• Descriptor: acidic fibroblast growth factor, SULFATE ION, FORMIC ACID, ... (4 entities in total)
• Functional Keywords: beta-trefoil, hormone-growth factor complex, hormone/growth factor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P05230
• Total number of polymer chains: 2
• Total formula weight: 33717.68

Authors

Brych, S.R.,Kim, J.,Spielmann, G.L.,Logan, T.M.,Blaber, M. (deposition date: 2002-06-17, release date: 2003-08-05, Last modification date: 2024-02-14)

Primary citation

Brych, S.R.,Kim, J.,Logan, T.M.,Blaber, M.
Accommodation of a highly symmetric core within a symmetric protein superfold
Protein Sci., 12:2704-2718, 2003

PubMed Abstract: An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF-1. This alternative group was designed so as to constrain the primary structure within the core region to the same threefold symmetry present in the tertiary structure of the protein fold (the beta-trefoil superfold). The alternative core is essentially indistinguishable from the WT core with regard to structure, stability, and folding kinetics. The results show that the beta-trefoil superfold is compatible with a threefold symmetric constraint on the core region, as might be the case if the superfold arose as a result of gene duplication/fusion events. Furthermore, this new core arrangement can form the basis of a structural "building block" that can greatly simplify the de novo design of beta-trefoil proteins by using symmetric structural complementarity. Remaining asymmetry within the core appears to be related to asymmetry in the tertiary structure associated with receptor and heparin binding functionality of the growth factor.

PubMed: 14627732
DOI: 10.1110/ps.03374903

Experimental method

X-RAY DIFFRACTION (1.7 Å)