1e1s: Difference between revisions

Revision as of 00:00, 1 July 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:1e1s.png

Template:STRUCTURE 1e1s

HUMAN PRION PROTEIN VARIANT S170NHUMAN PRION PROTEIN VARIANT S170N

Template:ABSTRACT PUBMED 10900000

About this StructureAbout this Structure

1E1S is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

NMR structures of three single-residue variants of the human prion protein., Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wuthrich K, Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5. PMID:10900000

Page seeded by OCA on Tue Jul 1 00:00:00 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1e1s.jpg|left|200px]]
+{{Seed}}
+[[Image:1e1s.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1e1s|  PDB=1e1s  |  SCENE=  }}
-'''HUMAN PRION PROTEIN VARIANT S170N'''
+===HUMAN PRION PROTEIN VARIANT S170N===
-==Overview==
+<!--
-The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in hPrP(S170N) it is with the corresponding Syrian hamster residue. All three substitutions are in the surface region of the structure of the cellular form of PrP (PrP(C)) that is formed by the C-terminal part of helix 3, with residues 218-230, and a loop of residues 166-172. This molecular region shows high species variability and has been implicated in specific interactions with a so far not further characterized "protein X," and it is related to the species barrier for transmission of prion diseases. As expected, the three variant hPrP(121-230) structures have the same global architecture as the previously determined wild-type bovine, human, murine, and Syrian hamster prion proteins, but with the present study two localized "conformational markers" could be related with single amino acid exchanges. These are the length and quality of definition of helix 3, and the NMR-observability of the residues in the loop 166-172. Poor definition of the C-terminal part of helix 3 is characteristic for murine PrP and has now been observed also for hPrP(R220K), and NMR observation of the complete loop 166-172 has so far been unique for Syrian hamster PrP and is now also documented for hPrP(S170N).
+The line below this paragraph, {{ABSTRACT_PUBMED_10900000}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10900000 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10900000}}
 ==About this Structure==
-E1S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1S OCA].
+E1S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1S OCA].
 ==Reference==
@@ Line 30: / Line 34: @@
 [[Category: Zahn, R.]]
 [[Category: Prion protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:33:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 00:00:00 2008''