Skip to main content

. 1967 Dec;58(6):2220–2226. doi: 10.1073/pnas.58.6.2220

THE STRUCTURE OF CARBOXYPEPTIDASE A, VI. SOME RESULTS AT 2.0-Å RESOLUTION, AND THE COMPLEX WITH GLYCYL-TYROSINE AT 2.8-Å RESOLUTION

G N Reeke ¹, J A Hartsuck ¹, M L Ludwig ¹, F A Quiocho ¹, T A Steitz ¹, W N Lipscomb ¹

PMCID: PMC223823 PMID: 16591584

2226

Images in this article

Image
on p.2221

Image
on p.2222

Image
on p.2223

Image
on p.2224

Image
on p.2225

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

BARGETZI J. P. KUMAR KS, COX DJ, WALSH KA, NEURATH H: THE AMINO ACID COMPOSITION OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. Biochemistry. 1963 Nov-Dec;2:1468–1474. doi: 10.1021/bi00906a046. [DOI] [PubMed] [Google Scholar]
BARGETZI J. P., THOMPSON E. O., SAMPATHKUMAR K. S., WALSH K. A., NEURATH H. THE AMINO- AND CARBOXYL-TERMINAL RESIDUES AND THE SELF-DIGESTION OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. J Biol Chem. 1964 Nov;239:3767–3774. [PubMed] [Google Scholar]
KUMAR K. S., CLEGG J. B., WALSH K. A. THE N-TERMINAL SEQUENCE OF BOVINE CARBOXYPEPTIDASE A AND ITS RELATION OF ZYMOGEN ACTIVATION. Biochemistry. 1964 Nov;3:1728–1732. doi: 10.1021/bi00899a024. [DOI] [PubMed] [Google Scholar]
NEURATH H. MECHANISM OF ZYMOGEN ACTIVATION. Fed Proc. 1964 Jan-Feb;23:1–7. [PubMed] [Google Scholar]
Némethy G., Phillips D. C., Leach S. J., Scheraga H. A. A second right-handed helical structure with the parameters of the Pauling-Corey alpha-helix. Nature. 1967 Apr 22;214(5086):363–365. doi: 10.1038/214363a0. [DOI] [PubMed] [Google Scholar]
PAULING L., COREY R. B., BRANSON H. R. The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain. Proc Natl Acad Sci U S A. 1951 Apr;37(4):205–211. doi: 10.1073/pnas.37.4.205. [DOI] [PMC free article] [PubMed] [Google Scholar]
Pauling L., Corey R. B. Configurations of Polypeptide Chains With Favored Orientations Around Single Bonds: Two New Pleated Sheets. Proc Natl Acad Sci U S A. 1951 Nov;37(11):729–740. doi: 10.1073/pnas.37.11.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
Riordan J. F., Sokolovsky M., Vallee B. L. Environmentally sensitive tyrosyl residues. Nitration with tetranitromethane. Biochemistry. 1967 Jan;6(1):358–361. doi: 10.1021/bi00853a053. [DOI] [PubMed] [Google Scholar]
Roholt O. A., Pressman D. The sequence around the active-center tyrosyl residue of bovine pancreatic carboxypeptidase A. Proc Natl Acad Sci U S A. 1967 Jul;58(1):280–285. doi: 10.1073/pnas.58.1.280. [DOI] [PMC free article] [PubMed] [Google Scholar]
SIMPSON R. T., RIORDAN J. F., VALLEE B. L. FUNCTIONAL TYROSYL RESIDUES IN THE ACTIVE CENTER OF BOVINE PANCREATIC CARBOXYPEPTIDASE A. Biochemistry. 1963 May-Jun;2:616–622. doi: 10.1021/bi00903a039. [DOI] [PubMed] [Google Scholar]
Simpson R. T., Vallee B. L. Iodocarboxypeptidase. Biochemistry. 1966 May;5(5):1760–1767. doi: 10.1021/bi00869a045. [DOI] [PubMed] [Google Scholar]
Steitz T. A., Ludwig M. L., Quiocho F. A., Lipscomb W. N. The structure of carboxypepidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 A resolution. J Biol Chem. 1967 Oct 25;242(20):4662–4668. [PubMed] [Google Scholar]
VALLEE B. L. ACTIVE CENTER OF CARBOXYPEPTIDASE A. Fed Proc. 1964 Jan-Feb;23:8–17. [PubMed] [Google Scholar]
WALSH K. A., SAMPATH KUMAR K. S., BARGETZI J. P., NEURATH H. Approaches to the selective chemical labeling of the active site of carboxypepticase A. Proc Natl Acad Sci U S A. 1962 Aug;48:1443–1449. doi: 10.1073/pnas.48.8.1443. [DOI] [PMC free article] [PubMed] [Google Scholar]

ACTIONS

RESOURCES