1RG8
Human Acidic Fibroblast Growth Factor (haFGF-1) at 1.10 angstrom resolution (140 amino acid form)
Summary for 1RG8
| Entry DOI | 10.2210/pdb1rg8/pdb |
| Descriptor | Heparin-binding growth factor 1, FORMIC ACID (3 entities in total) |
| Functional Keywords | beta-trefoil, hormone-growth factor complex, hormone/growth factor |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 33603.62 |
| Authors | Bernett, M.J.,Somasundaram, T.,Blaber, M. (deposition date: 2003-11-11, release date: 2004-10-05, Last modification date: 2023-08-23) |
| Primary citation | Bernett, M.J.,Somasundaram, T.,Blaber, M. An atomic resolution structure for human fibroblast growth factor 1. Proteins, 57:626-634, 2004 Cited by PubMed Abstract: A 1.10-A atomic resolution X-ray structure of human fibroblast growth factor 1 (FGF-1), a member of the beta-trefoil superfold, has been determined. The beta-trefoil is one of 10 fundamental protein superfolds and is the only superfold to exhibit 3-fold structural symmetry (comprising 3 "trefoil" units). The quality of the diffraction data permits unambiguous assignment of Asn, Gln, and His rotamers, Pro ring pucker, as well as refinement of atomic anisotropic displacement parameters (ADPs). The FGF-1 structure exhibits numerous core-packing defects, detectable using a 1.0-A probe radius. In addition to contributing to the relatively low thermal stability of FGF-1, these defects may also permit domain motions within the structure. The availability of refined ADPs allows a translation/libration/screw (TLS) analysis of putative rigid body domains. The TLS analysis shows that beta-strands 6-12 together form a rigid body, and there is a clear demarcation in TLS motions between the adjacent carboxyl- and amino-termini. Although separate from beta-strands 6-12, the individual beta-strands 1-5 do not exhibit correlated motions; thus, this region appears to be comparatively flexible. The heparin-binding contacts of FGF-1 are located within beta-strands 6-12; conversely, a significant portion of the receptor-binding contacts are located within beta-strands 1-5. Thus, the observed rigid body motion in FGF-1 appears related to the ligand-binding functionalities. PubMed: 15382229DOI: 10.1002/prot.20239 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.1 Å) |
Structure validation
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