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The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding.

Pickford AR, Smith SP, Staunton D, Boyd J, Campbell ID
EMBO J 20 1519-29 (2001)
Cited: 54 times
EuropePMC logo PMID: 11285216

Abstract

The solution structure of the (6)F1(1)F2(2)F2 fragment from the gelatin-binding region of fibronectin has been determined (Protein Data Bank entry codes 1e88 and 1e8b). The structure reveals an extensive hydrophobic interface between the non-contiguous (6)F1 and (2)F2 modules. The buried surface area between (6)F1 and (2)F2 ( approximately 870 A(2)) is the largest intermodule interface seen in fibronectin to date. The dissection of (6)F1(1)F2(2)F2 into the (6)F1(1)F2 pair and (2)F2 results in near-complete loss of gelatin-binding activity. The hairpin topology of (6)F1(1)F2(2)F2 may facilitate intramolecular contact between the matrix assembly regions flanking the gelatin-binding domain. This is the first high-resolution study to reveal a compact, globular arrangement of modules in fibronectin. This arrangement is not consistent with the view that fibronectin is simply a linear 'string of beads'.

Articles - 1e8b mentioned but not cited (3)

  1. The hairpin structure of the (6)F1(1)F2(2)F2 fragment from human fibronectin enhances gelatin binding. Pickford AR, Smith SP, Staunton D, Boyd J, Campbell ID. EMBO J. 20 1519-1529 (2001)
  2. Protein structure similarity from Principle Component Correlation analysis. Zhou X, Chou J, Wong ST. BMC Bioinformatics 7 40 (2006)
  3. A Novel In Silico Benchmarked Pipeline Capable of Complete Protein Analysis: A Possible Tool for Potential Drug Discovery. Perera DDBD, Perera KML, Peiris DC. Biology (Basel) 10 1113 (2021)


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