1a4y: Difference between revisions

Revision as of 16:08, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1a4y.png

Template:STRUCTURE 1a4y

RIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEXRIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEX

Template:ABSTRACT PUBMED 9311977

About this StructureAbout this Structure

1A4Y is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Molecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution., Papageorgiou AC, Shapiro R, Acharya KR, EMBO J. 1997 Sep 1;16(17):5162-77. PMID:9311977

Page seeded by OCA on Mon Jun 30 16:08:30 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1a4y.gif|left|200px]]
+{{Seed}}
+[[Image:1a4y.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1a4y|  PDB=1a4y  |  SCENE=  }}
-'''RIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEX'''
+===RIBONUCLEASE INHIBITOR-ANGIOGENIN COMPLEX===
-==Overview==
+<!--
-Human placental RNase inhibitor (hRI), a leucine-rich repeat protein, binds the blood vessel-inducing protein human angiogenin (Ang) with extraordinary affinity (Ki &lt;1 fM). Here we report a 2.0 A resolution crystal structure for the hRI-Ang complex that, together with extensive mutagenesis data from earlier studies, reveals the molecular features of this tight interaction. The hRI-Ang binding interface is large and encompasses 26 residues from hRI and 24 from Ang, recruited from multiple domains of both proteins. However, a substantial fraction of the energetically important contacts involve only a single region of each: the C-terminal segment 434-460 of hRI and the ribonucleolytic active centre of Ang, most notably the catalytic residue Lys40. Although the overall docking of Ang resembles that observed for RNase A in the crystal structure of its complex with the porcine RNase inhibitor, the vast majority of the interactions in the two complexes are distinctive, indicating that the broad specificity of the inhibitor for pancreatic RNase superfamily proteins is based largely on its capacity to recognize features unique to each of them. The implications of these findings for the development of small, hRI-based inhibitors of Ang for therapeutic use are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_9311977}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9311977 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9311977}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Hydrolase molecular recognition]]
 [[Category: Leucine-rich repeat]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:49:12 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:08:30 2008''