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1jv9

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(New page: 200px<br /><applet load="1jv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jv9" /> '''NMR Structure of BPTI Mutant G37A'''<br /> ...)
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[[Image:1jv9.gif|left|200px]]<br /><applet load="1jv9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jv9" />
 
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'''NMR Structure of BPTI Mutant G37A'''<br />
 
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==Overview==
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==NMR Structure of BPTI Mutant G37A==
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A point mutation, G37A, on the surface of bovine pancreatic trypsin, inhibitor (BPTI) destabilizes the protein by approximately 5 kcal/mol, which is very high for addition of one methyl group. In wild-type (WT), BPTI, Gly 37 HN is in an unusual NH-aromatic-NH network of interactions, with the ring of Tyr 35 and the side chain HN of Asn 44. G37A was designed, to disrupt this interaction, since the phi and psi backbone angles of G37, are not favorable for an amino acid containing a beta-carbon., Investigations of the structure and dynamics by NMR methods show that G37A, retains the average WT structure. The NH-aromatic-NH interactions remain, intact, as indicated by NOEs and the large upfield ring current shift, (approximately 4 ppm) of A37 HN. The NMR structure, confirmed by molecular, modeling calculations, requires phi and psi backbone angles that are, highly destabilizing when alanine is in position 37. Although the average, structure is essentially unchanged, the dynamics are altered dramatically., Many residues in the region of the mutation have increased flexibility, as, probed by aromatic ring flip rates and native state hydrogen exchange. We, conclude that a large fraction of the destabilization arises from, maintaining A37 in a high-energy conformation. This suggests that, disruption of the NH-aromatic-NH network is energetically very costly, and, may involve other cooperatively linked interactions. The results, illustrate the importance of the Gly-Gly sequence at positions 36 and 37, and the 37 HN-35 aromatic interaction to the stability, folding, and, dynamics of the BPTI.
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<StructureSection load='1jv9' size='340' side='right'caption='[[1jv9]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JV9 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jv9 OCA], [https://pdbe.org/1jv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jv9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/1jv9_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1jv9 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1JV9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JV9 OCA].
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*[[BPTI 3D structures|BPTI 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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A highly destabilizing mutation, G37A, of the bovine pancreatic trypsin inhibitor retains the average native conformation but greatly increases local flexibility., Battiste JL, Li R, Woodward C, Biochemistry. 2002 Feb 19;41(7):2237-45. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11841215 11841215]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Battiste, J.L.]]
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[[Category: Battiste JL]]
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[[Category: Li, R.]]
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[[Category: Li R]]
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[[Category: Woodward, C.]]
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[[Category: Woodward C]]
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[[Category: bpti]]
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[[Category: conformational strain]]
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[[Category: g37a mutant]]
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[[Category: minimized average structure]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:36:22 2007''
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Current revision

NMR Structure of BPTI Mutant G37A

PDB ID 1jv9

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