An atomic resolution structure for human fibroblast growth factor 1

被引:36
作者
Bernett, MJ
Somasundaram, T
Blaber, M [1 ]
机构
[1] Florida State Univ, Inst Mol Biophys, Kasha Lab 406, Tallahassee, FL 32306 USA
[2] Florida State Univ, Dept Chem & Biochem, Tallahassee, FL 32306 USA
关键词
atomic-resolution; anisotropic displacement; parameters; translation/libration/screw tensors; X-ray crystallography; fibroblast growth factor; beta-trefoil; protein dynamics;
D O I
10.1002/prot.20239
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A 1.10-Angstrom 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-Angstrom 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. (C) 2004 Wiley-Liss, Inc.
引用
收藏
页码:626 / 634
页数:9
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