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Literature DB >> 8895106

Amino acid sequence of the Phaseolus vulgaris var. "fogo na serra" inhibitor and interactive surface modeling for the enzyme-inhibitor complex.

P G de Carvalho¹, C Bloch, L Morhy, M C da Silva, L V de Mello, G Neshich.

Abstract

A trypsin and chymotrypsin inhibitor from seeds of Phaseolus vulgaris var. "Fogo na Serra" (PFSI) was purified and its complete amino acid sequence was determined using Edman degradation methods. The inhibitor was found to belong to the Bowman-Birk family of enzymatic inhibitors; it has 82 amino acid residues and a 8.985-kDa molecular mass. The PFSI/alpha-chymotrypsin binary complex has been modeled using the Turkey ovomucoid inhibitor third domain (OMTKY3) bound to alpha-chymotrypsin [Fujinaga et al. (1987), J. Mol. Biol., 195, 397-418. template. The model allowed identification of the binding surface.

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Year: 1996 PMID： 8895106 DOI： 10.1007/bf01908541

Source DB: PubMed Journal: J Protein Chem ISSN： 0277-8033

18 in total

1. WHAT IF: a molecular modeling and drug design program.

Authors: G Vriend
Journal: J Mol Graph Date: 1990-03

2. Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor.

Authors: M H Werner; D E Wemmer
Journal: J Mol Biol Date: 1992-06-05 Impact factor: 5.469

3. Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.

Authors: P Chen; J Rose; R Love; C H Wei; B C Wang
Journal: J Biol Chem Date: 1992-01-25 Impact factor: 5.157

4. Protein docking and complementarity.

Authors: B K Shoichet; I D Kuntz
Journal: J Mol Biol Date: 1991-09-05 Impact factor: 5.469

5. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes.

Authors: J W Ponder; F M Richards
Journal: J Mol Biol Date: 1987-02-20 Impact factor: 5.469

10. Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.

Authors: M Fujinaga; A R Sielecki; R J Read; W Ardelt; M Laskowski; M N James
Journal: J Mol Biol Date: 1987-05-20 Impact factor: 5.469

1 in total

1. Trypsin isoinhibitors with antiproliferative activity toward leukemia cells from Phaseolus vulgaris cv "White Cloud Bean".

Authors: Jian Sun; Hexiang Wang; Tzi Bun Ng
Journal: J Biomed Biotechnol Date: 2010-06-14

1 in total

Amino acid sequence of the Phaseolus vulgaris var. "fogo na serra" inhibitor and interactive surface modeling for the enzyme-inhibitor complex.

1. WHAT IF: a molecular modeling and drug design program.

2. Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor.

3. Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.

4. Protein docking and complementarity.

5. Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes.

6. Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins.

7. Solvent-accessible surfaces of proteins and nucleic acids.

8. 1H assignments and secondary structure determination of the soybean trypsin/chymotrypsin Bowman-Birk inhibitor.

9. On the size of the active site in proteases. I. Papain.

10. Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8 A resolution.

1. Trypsin isoinhibitors with antiproliferative activity toward leukemia cells from Phaseolus vulgaris cv "White Cloud Bean".