2004
DOI: 10.1016/j.str.2004.02.022
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: Erythroid spectrin, a major component of the cytoskeletal network of the red cell which contributes to both the stability and the elasticity of the red cell membrane, is composed of two subunits, alpha and beta, each formed by 16-20 tandem repeats. The properties of the repeats and their relative arrangement are thought to be key determinants of spectrin flexibility. Here we report a 2.4 A resolution crystal structure of human erythroid beta-spectrin repeats 8 and 9. This two-repeat fragment is unusual as it e… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

6
106
1

Year Published

2008
2008
2017
2017

Publication Types

Select...
5
2
1

Relationship

1
7

Authors

Journals

citations
Cited by 73 publications
(113 citation statements)
references
References 48 publications
6
106
1
Order By: Relevance
“…As has been observed with all other phased, multirepeat spectrin structures to date, adjacent repeats are connected with ␣-helical linkers. [32][33][34][35][36][37][38] As predicted by structurebased homology modeling and biophysical measurements, the crystal structure confirms a complex dominated by ␣-helices. Finally, although the aforementioned studies contributed significantly in modeling the interactions present at the tetramerization interface, it is only with the structure of this complex that the precise nature of the molecular interactions can be discerned (Figure 3).…”
Section: Structure Of the Spectrin ␣0-1/␤16-17 Complexsupporting
confidence: 55%
See 1 more Smart Citation
“…As has been observed with all other phased, multirepeat spectrin structures to date, adjacent repeats are connected with ␣-helical linkers. [32][33][34][35][36][37][38] As predicted by structurebased homology modeling and biophysical measurements, the crystal structure confirms a complex dominated by ␣-helices. Finally, although the aforementioned studies contributed significantly in modeling the interactions present at the tetramerization interface, it is only with the structure of this complex that the precise nature of the molecular interactions can be discerned (Figure 3).…”
Section: Structure Of the Spectrin ␣0-1/␤16-17 Complexsupporting
confidence: 55%
“…Among published structures of spectrins, the majority are 1-or 2-repeat fragments. [33][34][35][36][37][38][39]45,46 Three 3-repeat structures have been determined to date: chicken brain ␣-spectrin repeats 15-17, human brain ␤-spectrin repeats 14-16, and human erythroid ␤-spectrin repeats 13-15 (in complex with a fragment of ankyrin). 32,45,47 Although chicken brain ␣-spectrin repeats 15-17 are generally linear, both human brain ␤-spectrin repeats 14-16 and erythroid ␤-spectrin repeats 13-15 display a noticeable bend of approximately 50°between repeats 14 and 15.…”
Section: Comparison With Other Multirepeat Spectrin Structuresmentioning
confidence: 99%
“…The 14-15 linker connected helices 14C and 15A into a single long continuous ␣-helix similar to that observed in previous spectrin-like di-repeat structures. 35,36,38,39 Fourteen C-terminal residues (residues C 1892 -R 1907 ) and 13 residues in the 15A-B loop (residues L 1820 -H 1835 ) were disordered and could not be modeled.…”
Section: The Structure Of the Ankyrin-binding Domain Of ␤I-spectrinmentioning
confidence: 99%
“…7). Tworepeat fragments, HEβ89 (25) and CBα1617 (33), previously characterized by X-ray crystallography are also shown in Fig. 7 for comparison.…”
Section: Zu5 Forms a Complex With Heβ1315 And With Heβ1415 But Not Wimentioning
confidence: 99%
“…This reasoning also applies, of course, to the other prominent members of the spectrin family, α-actinin and dystrophin (30). It remains a mystery, however, as to what dictates this structural versatility of the signature spectrin repeating unit motif (31) in spite of the availability of Xray crystal structures of two (25,32,33) and three (34) repeat fragments of spectrin and α-actinin. An exception is the structure of four repeat fragments of α-actinin (35) with a lengthwise twist which enables interaction of α-actinin with actin at each end.…”
mentioning
confidence: 99%