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==RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)==
==RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)==
<StructureSection load='1mit' size='340' side='right'caption='[[1mit]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
<StructureSection load='1mit' size='340' side='right'caption='[[1mit]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Boston_marrow Boston marrow]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mit]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cucurbita_maxima Cucurbita maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MIT FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mit OCA], [https://pdbe.org/1mit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mit RCSB], [https://www.ebi.ac.uk/pdbsum/1mit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mit ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mit OCA], [https://pdbe.org/1mit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mit RCSB], [https://www.ebi.ac.uk/pdbsum/1mit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mit ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ITH5_CUCMA ITH5_CUCMA]] Specifically inhibits both trypsin and activated Hageman factor.  
[https://www.uniprot.org/uniprot/ITH5_CUCMA ITH5_CUCMA] Specifically inhibits both trypsin and activated Hageman factor.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mit ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mit ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of recombinant Cucurbita maxima trypsin inhibitor-V (rCMTI-V), whose N-terminal is unacetylated and carries an extra glycine residue, was determined by means of two-dimensional (2D) homo and 3D hetero NMR experiments in combination with a distance geometry and simulated annealing algorithm. A total of 927 interproton distances and 123 torsion angle constraints were utilized to generate 18 structures. The root mean squared deviation (RMSD) of the mean structure is 0.53 A for main-chain atoms and 0.95 A for all the non-hydrogen atoms of residues 3-40 and 49-67. The average structure of rCMTI-V is found to be almost the same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., &amp; Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. The backbone dynamics of uniformly 15N-labeled rCMTI-V were characterized by 2D 1H-15N NMR methods. 15N spin-lattice and spin-spin relaxation rate constants (R1 and R2, respectively) and [1H]-15N steady-state heteronuclear Overhauser effect enhancements were measured for the peptide NH units and, using the model-free formalism [Lipari, G., &amp; Szabo, A. (1982) J. Am. Chem. Soc. 104, 4546-4559, 4559-4570], the following parameters were determined: overall tumbling correlation time for the protein molecule (tau m), generalized order parameters for the individual N-H vectors (S2), effective correlation times for their internal motions (tau e), and terms to account for motions on a slower time scale (second) due to chemical exchange and/or conformational averaging (R(ex)). Most of the backbone NH groups of rCMTI-V are found to be highly constrained ((S2) = 0.83) with the exception of those in the binding loop (residues 41-48, (S2) = 0.71) and the N-terminal region ((S2) = 0.73). Main-chain atoms in these regions show large RMSD values in the average NMR structure. Residues involved in turns also appear to have more mobility ((S2) = 0.80). Dynamical properties of rCMTI-V were compared with those of two other inhibitors of the potato I family--eglin c [Peng, J. W., &amp; Wagner, G. (1992) Biochemistry 31, 8571-8586] and barley chymotrypsin inhibitor 2 [CI-2; Shaw, G. L., Davis, B., Keeler, J., &amp; Fersht, A. R. (1995) Biochemistry 34, 2225-2233]. The Cys3-Cys48 linkage found only in rCMTI-V appears to somewhat reduce the N-terminal flexibility; likewise, the C-terminal of rCMTI-V, being part of a beta-sheet, appears to be more rigid.
Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.,Liu J, Prakash O, Cai M, Gong Y, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R Biochemistry. 1996 Feb 6;35(5):1516-24. PMID:8634282<ref>PMID:8634282</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mit" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Boston marrow]]
[[Category: Cucurbita maxima]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Cai, M]]
[[Category: Cai M]]
[[Category: Gong, Y]]
[[Category: Gong Y]]
[[Category: Huang, J K]]
[[Category: Huang J-K]]
[[Category: Huang, Y]]
[[Category: Huang Y]]
[[Category: Krishnamoorthi, R]]
[[Category: Krishnamoorthi R]]
[[Category: Liu, J]]
[[Category: Liu J]]
[[Category: Prakash, O]]
[[Category: Prakash O]]
[[Category: Wen, J J]]
[[Category: Wen JJ]]
[[Category: Wen, L]]
[[Category: Wen L]]

Revision as of 11:36, 10 April 2024

RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)RECOMBINANT CUCURBITA MAXIMA TRYPSIN INHIBITOR V (RCMTI-V) (NMR, MINIMIZED AVERAGE STRUCTURE)

Structural highlights

1mit is a 1 chain structure with sequence from Cucurbita maxima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ITH5_CUCMA Specifically inhibits both trypsin and activated Hageman factor.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

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