1h53: Difference between revisions
No edit summary |
No edit summary |
||
| Line 27: | Line 27: | ||
[[Category: ribonuclease]] | [[Category: ribonuclease]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:29:01 2007'' | ||
Revision as of 16:24, 30 October 2007
|
BINDING OF PHOSPHATE AND PYROPHOSPHATE IONS AT THE ACTIVE SITE OF HUMAN ANGIOGENIN AS REVEALED BY X-RAY CRYSTALLOGRAPHY
OverviewOverview
Human angiogenin (Ang) is an unusual homolog of bovine pancreatic RNase A, that utilizes its ribonucleolytic activity to induce the formation of new, blood vessels. The pyrimidine-binding site of Ang was shown previously to, be blocked by glutamine 117, indicating that Ang must undergo a, conformational change to bind and cleave RNA. The mechanism and nature of, this change are not known, and no Ang-inhibitor complexes have been, characterized structurally thus far. Here, we report crystal structures, for the complexes of Ang with the inhibitors phosphate and pyrophosphate, and the structure of the complex of the superactive Ang variant Q117G with, phosphate, all at 2.0 A resolution. Phosphate binds to the catalytic site, of both Ang and Q117G in essentially the same manner observed in ... [(full description)]
About this StructureAbout this Structure
1H53 is a [Single protein] structure of sequence from [Homo sapiens] with PO4 and CIT as [ligands]. Structure known Active Sites: ACT and CIT. Full crystallographic information is available from [OCA].
ReferenceReference
Binding of phosphate and pyrophosphate ions at the active site of human angiogenin as revealed by X-ray crystallography., Leonidas DD, Chavali GB, Jardine AM, Li S, Shapiro R, Acharya KR, Protein Sci. 2001 Aug;10(8):1669-76. PMID:11468363
Page seeded by OCA on Tue Oct 30 15:29:01 2007