1TER

SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY

Summary for 1TER

• Entry DOI: 10.2210/pdb1ter/pdb
• Descriptor: TERTIAPIN (1 entity in total)
• Functional Keywords: toxin
• Biological source: Apis mellifera (honey bee)
• Cellular location: Secreted: P56587
• Total number of polymer chains: 1
• Total formula weight: 2464.14

Authors

Xu, X.,Nelson, J.W. (deposition date: 1994-04-08, release date: 1995-02-07, Last modification date: 2024-11-20)

Primary citation

Xu, X.,Nelson, J.W.
Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry.
Proteins, 17:124-137, 1993

PubMed Abstract: The solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures.

PubMed: 8265561
DOI: 10.1002/prot.340170203

Experimental method

SOLUTION NMR