1hym
From Proteopedia
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| - | [[Image:1hym.gif|left|200px]] | + | [[Image:1hym.gif|left|200px]] |
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| - | '''HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)''' | + | {{Structure |
| + | |PDB= 1hym |SIZE=350|CAPTION= <scene name='initialview01'>1hym</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HYM is a [ | + | 1HYM is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HYM OCA]. |
==Reference== | ==Reference== | ||
| - | Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure., Cai M, Gong Y, Prakash O, Krishnamoorthi R, Biochemistry. 1995 Sep 26;34(38):12087-94. PMID:[http:// | + | Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure., Cai M, Gong Y, Prakash O, Krishnamoorthi R, Biochemistry. 1995 Sep 26;34(38):12087-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7547948 7547948] |
[[Category: Cucurbita maxima]] | [[Category: Cucurbita maxima]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:10 2008'' |
Revision as of 09:43, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)
Overview
Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In comparison to the intact form, CMTI-V* exhibited markedly reduced inhibitory properties and binding affinities toward trypsin and human blood coagulation factor XIIa. The equilibrium constant of trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3 kcal.mol-1). From the temperature dependence of delta G degrees, the following thermodynamic parameters were estimated: delta H degrees = 1.6 kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the functional and thermodynamic differences between the two forms, the three-dimensional solution structure of CMTI-V* was determined by a combined approach of NMR, distance geometry, and simulated annealing methods. Thus, following sequence-specific and stereospecific resonance assignments, including those of beta-, gamma-, delta-, and epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances and 123 dihedral angle constraints were determined, resulting in the computation and energy-minimization of 20 structures for CMTI-V*. The average root mean squared deviation in position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)
About this Structure
1HYM is a Protein complex structure of sequences from Cucurbita maxima. Full crystallographic information is available from OCA.
Reference
Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure., Cai M, Gong Y, Prakash O, Krishnamoorthi R, Biochemistry. 1995 Sep 26;34(38):12087-94. PMID:7547948
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