1psp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1psp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psp, resolution 2.5&Aring;" /> '''PANCREATIC SPASMOLYTI...)
Line 1: Line 1:
-
[[Image:1psp.gif|left|200px]]<br /><applet load="1psp" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1psp.gif|left|200px]]<br /><applet load="1psp" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1psp, resolution 2.5&Aring;" />
caption="1psp, resolution 2.5&Aring;" />
'''PANCREATIC SPASMOLYTIC POLYPEPTIDE: FIRST THREE-DIMENSIONAL STRUCTURE OF A MEMBER OF THE MAMMALIAN TREFOIL FAMILY OF PEPTIDES'''<br />
'''PANCREATIC SPASMOLYTIC POLYPEPTIDE: FIRST THREE-DIMENSIONAL STRUCTURE OF A MEMBER OF THE MAMMALIAN TREFOIL FAMILY OF PEPTIDES'''<br />
==Overview==
==Overview==
-
BACKGROUND: The trefoil peptides are a rapidly growing family of peptides, mainly found in the gastrointestinal tract. There is circumstantial, evidence that they stabilize the mucus layer, and may affect the rate of, healing of the mucosal epithelium. RESULTS: We have determined the, structure of porcine pancreatic spasmolytic polypeptide (PSP) to 2.5 A, resolution. The polypeptide contains two trefoil domains. The domain, structure is compact, and is composed of a central short antiparallel, beta-sheet with one short helix above and one below it. This is a novel, motif. The two domains are related by two-fold symmetry, and each domain, contains a cleft. CONCLUSIONS: The cleft within each domain could, accommodate a polysaccharide chain, and may therefore be responsible for, binding mucin glycoproteins. We suggest that PSP may cross-link, glycoproteins, explaining its ability to stabilize the mucus layer.
+
BACKGROUND: The trefoil peptides are a rapidly growing family of peptides, mainly found in the gastrointestinal tract. There is circumstantial evidence that they stabilize the mucus layer, and may affect the rate of healing of the mucosal epithelium. RESULTS: We have determined the structure of porcine pancreatic spasmolytic polypeptide (PSP) to 2.5 A resolution. The polypeptide contains two trefoil domains. The domain structure is compact, and is composed of a central short antiparallel beta-sheet with one short helix above and one below it. This is a novel motif. The two domains are related by two-fold symmetry, and each domain contains a cleft. CONCLUSIONS: The cleft within each domain could accommodate a polysaccharide chain, and may therefore be responsible for binding mucin glycoproteins. We suggest that PSP may cross-link glycoproteins, explaining its ability to stabilize the mucus layer.
==About this Structure==
==About this Structure==
-
1PSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSP OCA].
+
1PSP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PSP OCA].
==Reference==
==Reference==
Line 16: Line 16:
[[Category: Gajhede, M.]]
[[Category: Gajhede, M.]]
[[Category: Henriksen, A.]]
[[Category: Henriksen, A.]]
-
[[Category: Petersen, J.F.W.]]
+
[[Category: Petersen, J F.W.]]
-
[[Category: Petersen, T.N.]]
+
[[Category: Petersen, T N.]]
[[Category: Thim, L.]]
[[Category: Thim, L.]]
-
[[Category: Wilson, K.S.]]
+
[[Category: Wilson, K S.]]
[[Category: spasmolytic protein]]
[[Category: spasmolytic protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:05:23 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:13 2008''

Revision as of 12:32, 21 February 2008


1psp, resolution 2.5Å

Drag the structure with the mouse to rotate

PANCREATIC SPASMOLYTIC POLYPEPTIDE: FIRST THREE-DIMENSIONAL STRUCTURE OF A MEMBER OF THE MAMMALIAN TREFOIL FAMILY OF PEPTIDES

Overview

BACKGROUND: The trefoil peptides are a rapidly growing family of peptides, mainly found in the gastrointestinal tract. There is circumstantial evidence that they stabilize the mucus layer, and may affect the rate of healing of the mucosal epithelium. RESULTS: We have determined the structure of porcine pancreatic spasmolytic polypeptide (PSP) to 2.5 A resolution. The polypeptide contains two trefoil domains. The domain structure is compact, and is composed of a central short antiparallel beta-sheet with one short helix above and one below it. This is a novel motif. The two domains are related by two-fold symmetry, and each domain contains a cleft. CONCLUSIONS: The cleft within each domain could accommodate a polysaccharide chain, and may therefore be responsible for binding mucin glycoproteins. We suggest that PSP may cross-link glycoproteins, explaining its ability to stabilize the mucus layer.

About this Structure

1PSP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.

Reference

Pancreatic spasmolytic polypeptide: first three-dimensional structure of a member of the mammalian trefoil family of peptides., Gajhede M, Petersen TN, Henriksen A, Petersen JF, Dauter Z, Wilson KS, Thim L, Structure. 1993 Dec 15;1(4):253-62. PMID:8081739

Page seeded by OCA on Thu Feb 21 14:32:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools