This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2pk4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pk4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pk4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pk4| PDB=2pk4 | SCENE= }}
{{STRUCTURE_2pk4| PDB=2pk4 | SCENE= }}
-
'''THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE'''
+
===THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE===
-
==Overview==
+
<!--
-
The crystallographic structure of the plasminogen kringle 4-epsilon-aminocaproic acid (ACA) complex (K4-ACA) has been solved by molecular replacement rotation-translation methods utilizing the refined apo-K4 structure as a search model (Mulichak et al., 1991), and it has been refined to an R value of 0.148 at 2.25-A resolution. The K4-ACA structure consists of two interkringle residues, the kringle along with the ACA ligand, and 106 water molecules. The lysine-binding site has been confirmed to be a relatively open and shallow depression, lined by aromatic rings of Trp62, Phe64, and Trp72, which provide a highly nonpolar environment between doubly charged anionic and cationic centers formed by Asp55/Asp57 and Lys35/Arg71. A zwitterionic ACA ligand molecule is held by hydrogen-bonded ion pair interactions and van der Waals contacts between the charged centers. The lysine-binding site of apo-K4 and K4-ACA have been compared: the rms differences in main-chain and side-chain positions are 0.25 and 0.69 A, respectively, both practically within error of the determinations. The largest deviations in the binding site are due to different crystal packing interactions. Thus, the lysine-binding site appears to be preformed, and lysine binding does not require conformational changes of the host. The results of NMR studies of lysine binding with K4 are correlated with the structure of K4-ACA and agree well.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1657149}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1657149 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1657149}}
==About this Structure==
==About this Structure==
Line 24: Line 28:
[[Category: Tulinsky, A.]]
[[Category: Tulinsky, A.]]
[[Category: Wu, T P.]]
[[Category: Wu, T P.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:16:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:30:54 2008''

Revision as of 12:30, 29 July 2008

Image:2pk4.png

Template:STRUCTURE 2pk4

THE REFINED STRUCTURE OF THE EPSILON-AMINOCAPROIC ACID COMPLEX OF HUMAN PLASMINOGEN KRINGLE

Template:ABSTRACT PUBMED 1657149

About this Structure

2PK4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The refined structure of the epsilon-aminocaproic acid complex of human plasminogen kringle 4., Wu TP, Padmanabhan K, Tulinsky A, Mulichak AM, Biochemistry. 1991 Oct 29;30(43):10589-94. PMID:1657149

Page seeded by OCA on Tue Jul 29 15:30:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pk4"
Personal tools