1jv8
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1jv8.jpg|left|200px]] | + | [[Image:1jv8.jpg|left|200px]] |
| - | + | ||
| - | '''NMR Structure of BPTI Mutant G37A''' | + | {{Structure |
| + | |PDB= 1jv8 |SIZE=350|CAPTION= <scene name='initialview01'>1jv8</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of BPTI Mutant G37A''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1JV8 is a [ | + | 1JV8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JV8 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/11841215 11841215] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 20: | Line 29: | ||
[[Category: g37a mutant]] | [[Category: g37a mutant]] | ||
| - | ''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 12:09:01 2008'' |
Revision as of 10:09, 20 March 2008
| |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR Structure of BPTI Mutant G37A
Overview
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.
About this Structure
1JV8 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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:11841215
Page seeded by OCA on Thu Mar 20 12:09:01 2008
